ID   COX5B_BOVIN             Reviewed;         129 AA.
AC   P00428; A6QL66; P11949; Q3T041;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   24-JAN-2024, entry version 186.
DE   RecName: Full=Cytochrome c oxidase subunit 5B, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide VIa;
DE   AltName: Full=Cytochrome c oxidase polypeptide Vb;
DE   Flags: Precursor;
GN   Name=COX5B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus, and Hereford;
RC   TISSUE=Heart ventricle, and Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 32-129.
RX   PubMed=6292069; DOI=10.1515/bchm2.1982.363.2.1141;
RA   Biewald R., Buse G.;
RT   "Studies on cytochrome c oxidase, IX. The primary structure of polypeptide
RT   VIa.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 363:1141-1153(1982).
RN   [3]
RP   PROTEIN SEQUENCE OF 32-57.
RC   TISSUE=Liver;
RX   PubMed=2844245; DOI=10.1021/bi00413a048;
RA   Yanamura W., Zhang Y.-Z., Takamiya S., Capaldi R.A.;
RT   "Tissue-specific differences between heart and liver cytochrome c
RT   oxidase.";
RL   Biochemistry 27:4909-4914(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 51-129.
RX   PubMed=2840351; DOI=10.1016/0378-1119(88)90411-8;
RA   Zeviani M., Sakoda S., Sherbany A., Nakase H., Rizzuto R., Samitt C.E.,
RA   Dimauro S., Schon E.A.;
RT   "Sequence of cDNAs encoding subunit Vb of human and bovine cytochrome c
RT   oxidase.";
RL   Gene 65:1-11(1988).
RN   [5]
RP   SUBUNIT.
RX   PubMed=26698328; DOI=10.1074/jbc.m115.680553;
RA   Shinzawa-Itoh K., Shimomura H., Yanagisawa S., Shimada S., Takahashi R.,
RA   Oosaki M., Ogura T., Tsukihara T.;
RT   "Purification of active respiratory supercomplex from bovine heart
RT   mitochondria enables functional studies.";
RL   J. Biol. Chem. 291:4178-4184(2016).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ZINC.
RX   PubMed=8638158; DOI=10.1126/science.272.5265.1136;
RA   Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H.,
RA   Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT   "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8
RT   A.";
RL   Science 272:1136-1144(1996).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC   TISSUE=Heart;
RX   PubMed=10089392; DOI=10.1107/s0907444998006362;
RA   Tomizaki T., Yamashita E., Yamaguchi H., Aoyama H., Tsukihara T.,
RA   Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT   "Structure analysis of bovine heart cytochrome c oxidase at 2.8 A
RT   resolution.";
RL   Acta Crystallogr. D 55:31-45(1999).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC   TISSUE=Heart;
RX   PubMed=10771420; DOI=10.1107/s0907444900002213;
RA   Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T.,
RA   Shinzawa-Itoh K., Nakashima R., Yoshikawa S.;
RT   "X-ray structure of azide-bound fully oxidized cytochrome c oxidase from
RT   bovine heart at 2.9 A resolution.";
RL   Acta Crystallogr. D 56:529-535(2000).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC.
RX   PubMed=20385840; DOI=10.1073/pnas.0910410107;
RA   Muramoto K., Ohta K., Shinzawa-Itoh K., Kanda K., Taniguchi M.,
RA   Nabekura H., Yamashita E., Tsukihara T., Yoshikawa S.;
RT   "Bovine cytochrome c oxidase structures enable O2 reduction with
RT   minimization of reactive oxygens and provide a proton-pumping gate.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:7740-7745(2010).
RN   [10]
RP   STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS).
RX   PubMed=27830641; DOI=10.7554/elife.21290;
RA   Sousa J.S., Mills D.J., Vonck J., Kuehlbrandt W.;
RT   "Functional asymmetry and electron flow in the bovine respirasome.";
RL   Elife 5:0-0(2016).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC.
RX   PubMed=27605664; DOI=10.1074/jbc.m115.711770;
RA   Yano N., Muramoto K., Shimada A., Takemura S., Baba J., Fujisawa H.,
RA   Mochizuki M., Shinzawa-Itoh K., Yamashita E., Tsukihara T., Yoshikawa S.;
RT   "The Mg2+-containing water cluster of mammalian cytochrome c oxidase
RT   collects four pumping proton equivalents in each catalytic cycle.";
RL   J. Biol. Chem. 291:23882-23894(2016).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX   PubMed=31533957; DOI=10.1073/pnas.1907183116;
RA   Shinzawa-Itoh K., Sugimura T., Misaki T., Tadehara Y., Yamamoto S.,
RA   Hanada M., Yano N., Nakagawa T., Uene S., Yamada T., Aoyama H.,
RA   Yamashita E., Tsukihara T., Yoshikawa S., Muramoto K.;
RT   "Monomeric structure of an active form of bovine cytochrome c oxidase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:19945-19951(2019).
CC   -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC       mitochondrial electron transport chain which drives oxidative
CC       phosphorylation. The respiratory chain contains 3 multisubunit
CC       complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC       cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC       CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC       transfer electrons derived from NADH and succinate to molecular oxygen,
CC       creating an electrochemical gradient over the inner membrane that
CC       drives transmembrane transport and the ATP synthase. Cytochrome c
CC       oxidase is the component of the respiratory chain that catalyzes the
CC       reduction of oxygen to water. Electrons originating from reduced
CC       cytochrome c in the intermembrane space (IMS) are transferred via the
CC       dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC       to the active site in subunit 1, a binuclear center (BNC) formed by
CC       heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC       water molecules using 4 electrons from cytochrome c in the IMS and 4
CC       protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P04037}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P04037}.
CC   -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC       multisubunit enzyme composed of 14 subunits. The complex is composed of
CC       a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC       the mitochondrial DNA, and 11 supernumerary subunits COX4I1 (or
CC       COX4I2), COX5A, COX5B, COX6A2 (or COX6A1), COX6B1 (or COX6B2), COX6C,
CC       COX7A1 (or COX7A2), COX7B, COX7C, COX8B and NDUFA4, which are encoded
CC       in the nuclear genome (PubMed:8638158). The complex exists as a monomer
CC       or a dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC       ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC       III, CIII), resulting in different assemblies (supercomplex
CC       SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:26698328,
CC       PubMed:27830641). {ECO:0000269|PubMed:26698328,
CC       ECO:0000269|PubMed:27830641, ECO:0000269|PubMed:8638158}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:27605664,
CC       ECO:0000269|PubMed:31533957}; Matrix side {ECO:0000269|PubMed:27605664,
CC       ECO:0000269|PubMed:31533957}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5B family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA30465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC102579; AAI02580.1; -; mRNA.
DR   EMBL; BC147855; AAI47856.1; -; mRNA.
DR   EMBL; M19962; AAA30465.1; ALT_INIT; mRNA.
DR   PIR; A00495; OGBO6A.
DR   RefSeq; NP_001029218.1; NM_001034046.2.
DR   PDB; 1OCC; X-ray; 2.80 A; F/S=32-129.
DR   PDB; 1OCO; X-ray; 2.80 A; F/S=32-129.
DR   PDB; 1OCR; X-ray; 2.35 A; F/S=32-129.
DR   PDB; 1OCZ; X-ray; 2.90 A; F/S=32-129.
DR   PDB; 1V54; X-ray; 1.80 A; F/S=32-129.
DR   PDB; 1V55; X-ray; 1.90 A; F/S=32-129.
DR   PDB; 2DYR; X-ray; 1.80 A; F/S=32-129.
DR   PDB; 2DYS; X-ray; 2.20 A; F/S=32-129.
DR   PDB; 2EIJ; X-ray; 1.90 A; F/S=32-129.
DR   PDB; 2EIK; X-ray; 2.10 A; F/S=32-129.
DR   PDB; 2EIL; X-ray; 2.10 A; F/S=32-129.
DR   PDB; 2EIM; X-ray; 2.60 A; F/S=32-129.
DR   PDB; 2EIN; X-ray; 2.70 A; F/S=32-129.
DR   PDB; 2OCC; X-ray; 2.30 A; F/S=32-129.
DR   PDB; 2Y69; X-ray; 1.95 A; F/S=1-129.
DR   PDB; 2YBB; EM; 19.00 A; Q=32-129.
DR   PDB; 2ZXW; X-ray; 2.50 A; F/S=32-129.
DR   PDB; 3ABK; X-ray; 2.00 A; F/S=32-129.
DR   PDB; 3ABL; X-ray; 2.10 A; F/S=32-129.
DR   PDB; 3ABM; X-ray; 1.95 A; F/S=32-129.
DR   PDB; 3AG1; X-ray; 2.20 A; F/S=32-129.
DR   PDB; 3AG2; X-ray; 1.80 A; F/S=32-129.
DR   PDB; 3AG3; X-ray; 1.80 A; F/S=32-129.
DR   PDB; 3AG4; X-ray; 2.05 A; F/S=32-129.
DR   PDB; 3ASN; X-ray; 3.00 A; F/S=32-129.
DR   PDB; 3ASO; X-ray; 2.30 A; F/S=32-129.
DR   PDB; 3WG7; X-ray; 1.90 A; F/S=32-129.
DR   PDB; 3X2Q; X-ray; 2.00 A; F/S=32-129.
DR   PDB; 5B1A; X-ray; 1.50 A; F/S=32-129.
DR   PDB; 5B1B; X-ray; 1.60 A; F/S=32-129.
DR   PDB; 5B3S; X-ray; 1.68 A; F/S=32-129.
DR   PDB; 5GPN; EM; 5.40 A; 3=32-129.
DR   PDB; 5IY5; X-ray; 2.00 A; F/S=32-129.
DR   PDB; 5LUF; EM; 9.10 A; 3=32-129.
DR   PDB; 5W97; X-ray; 2.30 A; F/f=32-129.
DR   PDB; 5WAU; X-ray; 1.95 A; F/f=32-129.
DR   PDB; 5X19; X-ray; 2.20 A; F/S=32-129.
DR   PDB; 5X1B; X-ray; 2.40 A; F/S=32-129.
DR   PDB; 5X1F; X-ray; 2.20 A; F/S=32-129.
DR   PDB; 5XDQ; X-ray; 1.77 A; F/S=32-125.
DR   PDB; 5XDX; X-ray; 1.99 A; F/S=32-125.
DR   PDB; 5XTH; EM; 3.90 A; 2=32-129.
DR   PDB; 5XTI; EM; 17.40 A; 2/B2=32-129.
DR   PDB; 5Z84; X-ray; 1.85 A; F/S=32-129.
DR   PDB; 5Z85; X-ray; 1.85 A; F/S=32-129.
DR   PDB; 5Z86; X-ray; 1.85 A; F/S=32-129.
DR   PDB; 5ZCO; X-ray; 1.90 A; F/S=32-129.
DR   PDB; 5ZCP; X-ray; 1.65 A; F/S=32-129.
DR   PDB; 5ZCQ; X-ray; 1.65 A; F/S=32-129.
DR   PDB; 6J8M; X-ray; 1.90 A; F/S=32-129.
DR   PDB; 6JUW; X-ray; 1.80 A; F/S=32-129.
DR   PDB; 6JY3; X-ray; 1.85 A; F=32-129.
DR   PDB; 6JY4; X-ray; 1.95 A; F=32-129.
DR   PDB; 6NKN; X-ray; 2.50 A; F/S=32-129.
DR   PDB; 6NMF; X-ray; 2.80 A; F/S=32-129.
DR   PDB; 6NMP; X-ray; 2.90 A; F/S=32-129.
DR   PDB; 7COH; X-ray; 1.30 A; F/S=32-129.
DR   PDB; 7CP5; X-ray; 1.76 A; F/S=32-125.
DR   PDB; 7D5W; X-ray; 1.84 A; F/S=32-125.
DR   PDB; 7D5X; X-ray; 1.74 A; F/S=32-125.
DR   PDB; 7DGQ; EM; 5.00 A; A5=1-129.
DR   PDB; 7DGR; EM; 4.60 A; A6=1-129.
DR   PDB; 7DGS; EM; 7.80 A; B2=1-129.
DR   PDB; 7DKF; EM; 8.30 A; F3=1-129.
DR   PDB; 7EV7; X-ray; 1.70 A; F/S=32-129.
DR   PDB; 7THU; X-ray; 1.93 A; FFF/SSS=32-129.
DR   PDB; 7TIE; X-ray; 1.90 A; FFF/SSS=32-129.
DR   PDB; 7TIH; X-ray; 2.35 A; FFF/SSS=32-129.
DR   PDB; 7TII; X-ray; 2.45 A; FFF/SSS=32-129.
DR   PDB; 7VUW; X-ray; 1.60 A; F/S=32-125.
DR   PDB; 7VVR; X-ray; 1.65 A; F/S=32-125.
DR   PDB; 7W3E; X-ray; 1.45 A; F/S=33-125.
DR   PDB; 7XMA; X-ray; 2.20 A; F/S=32-129.
DR   PDB; 7XMB; X-ray; 2.20 A; F/S=32-129.
DR   PDB; 7Y44; X-ray; 1.90 A; F/S=32-129.
DR   PDB; 7YPY; X-ray; 1.50 A; F/S=32-129.
DR   PDB; 8D4T; EM; 3.10 A; S=35-125.
DR   PDB; 8GBT; X-ray; 2.80 A; F/S=32-129.
DR   PDB; 8GCQ; X-ray; 2.38 A; F/S=32-129.
DR   PDB; 8GVM; X-ray; 1.85 A; F/S=32-129.
DR   PDB; 8H8R; X-ray; 1.70 A; F/S=32-129.
DR   PDB; 8H8S; X-ray; 1.70 A; F/S=32-129.
DR   PDB; 8IJN; X-ray; 1.80 A; F/S=32-129.
DR   PDBsum; 1OCC; -.
DR   PDBsum; 1OCO; -.
DR   PDBsum; 1OCR; -.
DR   PDBsum; 1OCZ; -.
DR   PDBsum; 1V54; -.
DR   PDBsum; 1V55; -.
DR   PDBsum; 2DYR; -.
DR   PDBsum; 2DYS; -.
DR   PDBsum; 2EIJ; -.
DR   PDBsum; 2EIK; -.
DR   PDBsum; 2EIL; -.
DR   PDBsum; 2EIM; -.
DR   PDBsum; 2EIN; -.
DR   PDBsum; 2OCC; -.
DR   PDBsum; 2Y69; -.
DR   PDBsum; 2YBB; -.
DR   PDBsum; 2ZXW; -.
DR   PDBsum; 3ABK; -.
DR   PDBsum; 3ABL; -.
DR   PDBsum; 3ABM; -.
DR   PDBsum; 3AG1; -.
DR   PDBsum; 3AG2; -.
DR   PDBsum; 3AG3; -.
DR   PDBsum; 3AG4; -.
DR   PDBsum; 3ASN; -.
DR   PDBsum; 3ASO; -.
DR   PDBsum; 3WG7; -.
DR   PDBsum; 3X2Q; -.
DR   PDBsum; 5B1A; -.
DR   PDBsum; 5B1B; -.
DR   PDBsum; 5B3S; -.
DR   PDBsum; 5GPN; -.
DR   PDBsum; 5IY5; -.
DR   PDBsum; 5LUF; -.
DR   PDBsum; 5W97; -.
DR   PDBsum; 5WAU; -.
DR   PDBsum; 5X19; -.
DR   PDBsum; 5X1B; -.
DR   PDBsum; 5X1F; -.
DR   PDBsum; 5XDQ; -.
DR   PDBsum; 5XDX; -.
DR   PDBsum; 5XTH; -.
DR   PDBsum; 5XTI; -.
DR   PDBsum; 5Z84; -.
DR   PDBsum; 5Z85; -.
DR   PDBsum; 5Z86; -.
DR   PDBsum; 5ZCO; -.
DR   PDBsum; 5ZCP; -.
DR   PDBsum; 5ZCQ; -.
DR   PDBsum; 6J8M; -.
DR   PDBsum; 6JUW; -.
DR   PDBsum; 6JY3; -.
DR   PDBsum; 6JY4; -.
DR   PDBsum; 6NKN; -.
DR   PDBsum; 6NMF; -.
DR   PDBsum; 6NMP; -.
DR   PDBsum; 7COH; -.
DR   PDBsum; 7CP5; -.
DR   PDBsum; 7D5W; -.
DR   PDBsum; 7D5X; -.
DR   PDBsum; 7DGQ; -.
DR   PDBsum; 7DGR; -.
DR   PDBsum; 7DGS; -.
DR   PDBsum; 7DKF; -.
DR   PDBsum; 7EV7; -.
DR   PDBsum; 7THU; -.
DR   PDBsum; 7TIE; -.
DR   PDBsum; 7TIH; -.
DR   PDBsum; 7TII; -.
DR   PDBsum; 7VUW; -.
DR   PDBsum; 7VVR; -.
DR   PDBsum; 7W3E; -.
DR   PDBsum; 7XMA; -.
DR   PDBsum; 7XMB; -.
DR   PDBsum; 7Y44; -.
DR   PDBsum; 7YPY; -.
DR   PDBsum; 8D4T; -.
DR   PDBsum; 8GBT; -.
DR   PDBsum; 8GCQ; -.
DR   PDBsum; 8GVM; -.
DR   PDBsum; 8H8R; -.
DR   PDBsum; 8H8S; -.
DR   PDBsum; 8IJN; -.
DR   AlphaFoldDB; P00428; -.
DR   EMDB; EMD-27196; -.
DR   EMDB; EMD-30673; -.
DR   EMDB; EMD-30674; -.
DR   EMDB; EMD-30675; -.
DR   EMDB; EMD-30706; -.
DR   EMDB; EMD-4107; -.
DR   EMDB; EMD-9534; -.
DR   SMR; P00428; -.
DR   CORUM; P00428; -.
DR   DIP; DIP-38985N; -.
DR   IntAct; P00428; 3.
DR   STRING; 9913.ENSBTAP00000068000; -.
DR   iPTMnet; P00428; -.
DR   PaxDb; 9913-ENSBTAP00000024678; -.
DR   GeneID; 287012; -.
DR   KEGG; bta:287012; -.
DR   CTD; 1329; -.
DR   eggNOG; KOG3352; Eukaryota.
DR   HOGENOM; CLU_127178_0_0_1; -.
DR   InParanoid; P00428; -.
DR   OrthoDB; 1320at2759; -.
DR   TreeFam; TF105063; -.
DR   BRENDA; 7.1.1.9; 908.
DR   UniPathway; UPA00705; -.
DR   EvolutionaryTrace; P00428; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   CDD; cd00924; Cyt_c_Oxidase_Vb; 1.
DR   Gene3D; 2.60.11.10; Cytochrome c oxidase, subunit Vb; 1.
DR   InterPro; IPR002124; Cyt_c_oxidase_su5b.
DR   InterPro; IPR036972; Cyt_c_oxidase_su5b_sf.
DR   PANTHER; PTHR10122; CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10122:SF20; CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL; 1.
DR   Pfam; PF01215; COX5B; 1.
DR   SUPFAM; SSF57802; Rubredoxin-like; 1.
DR   PROSITE; PS00848; COX5B_1; 1.
DR   PROSITE; PS51359; COX5B_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2844245,
FT                   ECO:0000269|PubMed:6292069"
FT   CHAIN           32..129
FT                   /note="Cytochrome c oxidase subunit 5B, mitochondrial"
FT                   /id="PRO_0000197028"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:20385840,
FT                   ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:8638158"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:20385840,
FT                   ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:8638158"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:20385840,
FT                   ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:8638158"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:20385840,
FT                   ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:8638158"
FT   MOD_RES         68
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19536"
FT   MOD_RES         86
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19536"
FT   MOD_RES         121
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19536"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   STRAND          83..91
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:1OCZ"
FT   STRAND          101..109
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:1OCC"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   STRAND          119..123
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:5W97"
SQ   SEQUENCE   129 AA;  13834 MW;  C78CE7552CE6C313 CRC64;
     MASRLLRGVG ALASQALRAR GPNGVSVVRS MASGGGVPTD EEQATGLERE VMLAARKGQD
     PYNILAPKAT SGTKEDPNLV PSITNKRIVG CICEEDNSTV IWFWLHKGEA QRCPSCGTHY
     KLVPHQLAH
//