Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Streptavidin

Gene
N/A
Organism
Streptomyces avidinii
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671Biotin
Binding sitei78 – 781Biotin
Binding sitei116 – 1161Biotin
Binding sitei132 – 1321Biotin
Binding sitei144 – 1441Biotin

Keywords - Ligandi

Biotin

Enzyme and pathway databases

SABIO-RKP22629.

Names & Taxonomyi

Protein namesi
Recommended name:
Streptavidin
OrganismiStreptomyces avidinii
Taxonomic identifieri1895 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 183159StreptavidinPRO_0000002729Add
BLAST

Proteomic databases

PRIDEiP22629.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
183
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni39 – 413Combined sources
Beta strandi43 – 475Combined sources
Beta strandi48 – 503Combined sources
Beta strandi52 – 576Combined sources
Beta strandi61 – 688Combined sources
Beta strandi70 – 734Combined sources
Helixi74 – 763Combined sources
Beta strandi78 – 847Combined sources
Beta strandi90 – 923Combined sources
Beta strandi95 – 10410Combined sources
Beta strandi109 – 12113Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi127 – 13610Combined sources
Helixi140 – 1456Combined sources
Beta strandi147 – 15610Combined sources
Helixi161 – 1699Combined sources
Beta strandi172 – 1765Combined sources
Helixi178 – 1803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DF8X-ray1.51A/B37-163[»]
1HQQX-ray1.70A/B/C/D36-163[»]
1HXLX-ray1.80A/B36-163[»]
1HXZX-ray1.80A/B36-163[»]
1HY2X-ray2.00A/B/C/D36-163[»]
1I9HX-ray2.40A/B25-163[»]
1KFFX-ray1.90A/B/C/D38-163[»]
1KL3X-ray1.70A/B/C/D38-163[»]
1KL4X-ray1.70A/B/C/D38-163[»]
1KL5X-ray1.80A/B/C/D38-163[»]
1LCVX-ray2.30A/B39-159[»]
1LCWX-ray2.20A/B39-159[»]
1LCZX-ray1.95A/B25-159[»]
1LUQX-ray0.96A/B37-163[»]
1MEPX-ray1.65A/B/C/D37-163[»]
1MK5X-ray1.40A/B37-163[»]
1MM9X-ray1.66A37-163[»]
1MOYX-ray1.55A37-163[»]
1N43X-ray1.89A/B/C/D37-163[»]
1N4JX-ray2.18A37-163[»]
1N7YX-ray1.96A/B/C/D37-163[»]
1N9MX-ray1.60A/B/C/D37-163[»]
1N9YX-ray1.53A/B/C/D37-163[»]
1NBXX-ray1.70A/B/C/D37-163[»]
1NC9X-ray1.80A/B/C/D37-163[»]
1NDJX-ray1.81A/B/C/D37-163[»]
1NQMX-ray1.70A/B/C/D24-159[»]
1PTSX-ray2.00A/B37-157[»]
1RSTX-ray1.70B38-163[»]
1RSUX-ray1.70B38-163[»]
1RXHX-ray2.90A/B37-163[»]
1RXJX-ray1.14A/B/C/D39-159[»]
1RXKX-ray1.70A/B38-159[»]
1SLDX-ray2.50B25-159[»]
1SLEX-ray2.00B/D25-159[»]
1SLFX-ray1.76B/D25-159[»]
1SLGX-ray1.76B/D25-159[»]
1SREX-ray1.78A/B37-157[»]
1SRFX-ray2.00A/B37-157[»]
1SRGX-ray1.80A/B37-157[»]
1SRHX-ray2.20A/B37-157[»]
1SRIX-ray1.65A/B37-157[»]
1SRJX-ray1.80A/B37-157[»]
1STPX-ray2.60A25-183[»]
1STRX-ray1.80B/D37-159[»]
1STSX-ray1.95B/D37-159[»]
1SWAX-ray1.90A/B/C/D37-163[»]
1SWBX-ray1.85A/B/C/D37-163[»]
1SWCX-ray1.80A/B/C/D37-163[»]
1SWDX-ray1.90A/B/C/D37-163[»]
1SWEX-ray2.06A/B/C/D37-163[»]
1SWFX-ray2.00A/B/C/D75-163[»]
1SWGX-ray1.80A/B/C/D75-178[»]
1SWHX-ray1.70A/B/C/D37-163[»]
1SWJX-ray2.00A/B/C/D37-163[»]
1SWKX-ray2.00A/B/C/D37-163[»]
1SWLX-ray1.80A/B/C/D37-163[»]
1SWNX-ray2.20A/B/C/D37-163[»]
1SWOX-ray1.95A/B/C/D37-163[»]
1SWPX-ray2.00A/B/C/D37-163[»]
1SWQX-ray1.90A/B/C/D37-163[»]
1SWRX-ray1.90A/B/C/D37-163[»]
1SWSX-ray2.00A/B/C/D37-163[»]
1SWTX-ray2.00A/B37-163[»]
1SWUX-ray1.14A/B/C/D37-163[»]
1VWAX-ray1.85B/D37-159[»]
1VWBX-ray1.82B37-159[»]
1VWCX-ray1.86B37-159[»]
1VWDX-ray1.87B37-159[»]
1VWEX-ray1.50B37-159[»]
1VWFX-ray1.92B37-159[»]
1VWGX-ray1.46B37-159[»]
1VWHX-ray1.48B37-159[»]
1VWIX-ray1.50B/D37-159[»]
1VWJX-ray1.45B/D37-159[»]
1VWKX-ray1.45B/D37-159[»]
1VWLX-ray1.45B/D37-159[»]
1VWMX-ray1.60B37-159[»]
1VWNX-ray1.85B37-159[»]
1VWOX-ray1.65B37-159[»]
1VWPX-ray1.75B37-159[»]
1VWQX-ray1.70B37-159[»]
1VWRX-ray1.50B37-159[»]
2BC3X-ray1.54A/B38-183[»]
2F01X-ray0.85A/B37-163[»]
2G5LX-ray1.15A/B37-163[»]
2GH7X-ray1.00A/B37-163[»]
2IZAX-ray1.46A37-157[»]
2IZBX-ray1.20A37-158[»]
2IZCX-ray1.40B/D37-159[»]
2IZDX-ray1.60B/D37-159[»]
2IZEX-ray1.57B/D37-159[»]
2IZFX-ray1.58B/D37-159[»]
2IZGX-ray1.36B/D37-159[»]
2IZHX-ray1.36B/D37-159[»]
2IZIX-ray1.50A37-159[»]
2IZJX-ray1.30A37-159[»]
2IZKX-ray1.30A37-159[»]
2IZLX-ray1.48B/D37-159[»]
2QCBX-ray1.65A38-183[»]
2RTAX-ray1.39A25-159[»]
2RTBX-ray1.50B/D25-159[»]
2RTCX-ray1.50B/D25-159[»]
2RTDX-ray1.65B/D25-159[»]
2RTEX-ray1.50B/D25-159[»]
2RTFX-ray1.47B/D25-159[»]
2RTGX-ray1.39B/D25-159[»]
2RTHX-ray1.56B/D25-159[»]
2RTIX-ray1.40B/D25-159[»]
2RTJX-ray1.40A25-159[»]
2RTKX-ray1.82A25-159[»]
2RTLX-ray1.41A25-159[»]
2RTMX-ray1.30A25-159[»]
2RTNX-ray1.80B/D25-159[»]
2RTOX-ray1.58B/D25-159[»]
2RTPX-ray1.50B/D25-159[»]
2RTQX-ray1.39B/D25-159[»]
2RTRX-ray1.62B/D25-159[»]
2WPUX-ray1.92A38-183[»]
2Y3EX-ray1.45A/B37-163[»]
2Y3FX-ray1.49A37-163[»]
3MG5X-ray1.30A/B/C/D37-163[»]
3PK2X-ray1.90A38-183[»]
3RDMX-ray1.60A37-164[»]
3RDOX-ray1.40A37-164[»]
3RDQX-ray1.60A37-164[»]
3RDSX-ray1.50A37-164[»]
3RDUX-ray1.50A37-164[»]
3RDXX-ray2.10A/B37-164[»]
3RE5X-ray1.95A37-164[»]
3RE6X-ray1.82A37-164[»]
3RY1X-ray1.03A/B/C/D37-163[»]
3RY2X-ray0.95A/B37-163[»]
3T6FX-ray1.22A/B37-163[»]
3T6LX-ray1.30A37-163[»]
3WYPX-ray1.30A/B/C/D37-163[»]
3WYQX-ray1.00A/B37-163[»]
4BX5X-ray1.43A/C37-72[»]
B/D37-163[»]
4BX6X-ray1.60A/B/C/D37-163[»]
4BX7X-ray2.26A/B37-163[»]
4CPEX-ray1.06A/B37-163[»]
4CPFX-ray1.14A/B37-163[»]
4CPHX-ray1.64A/B/C/D37-163[»]
4CPIX-ray1.54A/B/C/D37-163[»]
4DNEX-ray1.88A/B1-183[»]
4EKVX-ray2.00A25-183[»]
4GD9X-ray1.50A/B/C/D37-163[»]
4GDAX-ray1.00A/B37-163[»]
4GJSX-ray1.85A/B38-183[»]
4GJVX-ray2.40A38-183[»]
4IRWX-ray1.40A36-163[»]
4JO6X-ray1.75A/B/C/D25-183[»]
4OKAX-ray2.50A38-183[»]
ProteinModelPortaliP22629.
SMRiP22629. Positions 38-159.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22629.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 159123Avidin-likePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi83 – 853Cell attachment site; atypical

Sequence similaritiesi

Belongs to the avidin/streptavidin family.Curated
Contains 1 avidin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.40.128.30. 1 hit.
InterProiIPR005469. Avidin.
IPR017889. Avidin-like_CS.
IPR005468. Avidin/str.
[Graphical view]
PfamiPF01382. Avidin. 1 hit.
[Graphical view]
PRINTSiPR00709. AVIDIN.
SUPFAMiSSF50876. SSF50876. 1 hit.
PROSITEiPS00577. AVIDIN_1. 1 hit.
PS51326. AVIDIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22629-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKIVVAAIA VSLTTVSITA SASADPSKDS KAQVSAAEAG ITGTWYNQLG
60 70 80 90 100
STFIVTAGAD GALTGTYESA VGNAESRYVL TGRYDSAPAT DGSGTALGWT
110 120 130 140 150
VAWKNNYRNA HSATTWSGQY VGGAEARINT QWLLTSGTTE ANAWKSTLVG
160 170 180
HDTFTKVKPS AASIDAAKKA GVNNGNPLDA VQQ
Length:183
Mass (Da):18,834
Last modified:July 31, 1991 - v1
Checksum:i4652D8AE018468F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03591 Genomic DNA. Translation: CAA27265.1.
PIRiA23513.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03591 Genomic DNA. Translation: CAA27265.1.
PIRiA23513.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DF8X-ray1.51A/B37-163[»]
1HQQX-ray1.70A/B/C/D36-163[»]
1HXLX-ray1.80A/B36-163[»]
1HXZX-ray1.80A/B36-163[»]
1HY2X-ray2.00A/B/C/D36-163[»]
1I9HX-ray2.40A/B25-163[»]
1KFFX-ray1.90A/B/C/D38-163[»]
1KL3X-ray1.70A/B/C/D38-163[»]
1KL4X-ray1.70A/B/C/D38-163[»]
1KL5X-ray1.80A/B/C/D38-163[»]
1LCVX-ray2.30A/B39-159[»]
1LCWX-ray2.20A/B39-159[»]
1LCZX-ray1.95A/B25-159[»]
1LUQX-ray0.96A/B37-163[»]
1MEPX-ray1.65A/B/C/D37-163[»]
1MK5X-ray1.40A/B37-163[»]
1MM9X-ray1.66A37-163[»]
1MOYX-ray1.55A37-163[»]
1N43X-ray1.89A/B/C/D37-163[»]
1N4JX-ray2.18A37-163[»]
1N7YX-ray1.96A/B/C/D37-163[»]
1N9MX-ray1.60A/B/C/D37-163[»]
1N9YX-ray1.53A/B/C/D37-163[»]
1NBXX-ray1.70A/B/C/D37-163[»]
1NC9X-ray1.80A/B/C/D37-163[»]
1NDJX-ray1.81A/B/C/D37-163[»]
1NQMX-ray1.70A/B/C/D24-159[»]
1PTSX-ray2.00A/B37-157[»]
1RSTX-ray1.70B38-163[»]
1RSUX-ray1.70B38-163[»]
1RXHX-ray2.90A/B37-163[»]
1RXJX-ray1.14A/B/C/D39-159[»]
1RXKX-ray1.70A/B38-159[»]
1SLDX-ray2.50B25-159[»]
1SLEX-ray2.00B/D25-159[»]
1SLFX-ray1.76B/D25-159[»]
1SLGX-ray1.76B/D25-159[»]
1SREX-ray1.78A/B37-157[»]
1SRFX-ray2.00A/B37-157[»]
1SRGX-ray1.80A/B37-157[»]
1SRHX-ray2.20A/B37-157[»]
1SRIX-ray1.65A/B37-157[»]
1SRJX-ray1.80A/B37-157[»]
1STPX-ray2.60A25-183[»]
1STRX-ray1.80B/D37-159[»]
1STSX-ray1.95B/D37-159[»]
1SWAX-ray1.90A/B/C/D37-163[»]
1SWBX-ray1.85A/B/C/D37-163[»]
1SWCX-ray1.80A/B/C/D37-163[»]
1SWDX-ray1.90A/B/C/D37-163[»]
1SWEX-ray2.06A/B/C/D37-163[»]
1SWFX-ray2.00A/B/C/D75-163[»]
1SWGX-ray1.80A/B/C/D75-178[»]
1SWHX-ray1.70A/B/C/D37-163[»]
1SWJX-ray2.00A/B/C/D37-163[»]
1SWKX-ray2.00A/B/C/D37-163[»]
1SWLX-ray1.80A/B/C/D37-163[»]
1SWNX-ray2.20A/B/C/D37-163[»]
1SWOX-ray1.95A/B/C/D37-163[»]
1SWPX-ray2.00A/B/C/D37-163[»]
1SWQX-ray1.90A/B/C/D37-163[»]
1SWRX-ray1.90A/B/C/D37-163[»]
1SWSX-ray2.00A/B/C/D37-163[»]
1SWTX-ray2.00A/B37-163[»]
1SWUX-ray1.14A/B/C/D37-163[»]
1VWAX-ray1.85B/D37-159[»]
1VWBX-ray1.82B37-159[»]
1VWCX-ray1.86B37-159[»]
1VWDX-ray1.87B37-159[»]
1VWEX-ray1.50B37-159[»]
1VWFX-ray1.92B37-159[»]
1VWGX-ray1.46B37-159[»]
1VWHX-ray1.48B37-159[»]
1VWIX-ray1.50B/D37-159[»]
1VWJX-ray1.45B/D37-159[»]
1VWKX-ray1.45B/D37-159[»]
1VWLX-ray1.45B/D37-159[»]
1VWMX-ray1.60B37-159[»]
1VWNX-ray1.85B37-159[»]
1VWOX-ray1.65B37-159[»]
1VWPX-ray1.75B37-159[»]
1VWQX-ray1.70B37-159[»]
1VWRX-ray1.50B37-159[»]
2BC3X-ray1.54A/B38-183[»]
2F01X-ray0.85A/B37-163[»]
2G5LX-ray1.15A/B37-163[»]
2GH7X-ray1.00A/B37-163[»]
2IZAX-ray1.46A37-157[»]
2IZBX-ray1.20A37-158[»]
2IZCX-ray1.40B/D37-159[»]
2IZDX-ray1.60B/D37-159[»]
2IZEX-ray1.57B/D37-159[»]
2IZFX-ray1.58B/D37-159[»]
2IZGX-ray1.36B/D37-159[»]
2IZHX-ray1.36B/D37-159[»]
2IZIX-ray1.50A37-159[»]
2IZJX-ray1.30A37-159[»]
2IZKX-ray1.30A37-159[»]
2IZLX-ray1.48B/D37-159[»]
2QCBX-ray1.65A38-183[»]
2RTAX-ray1.39A25-159[»]
2RTBX-ray1.50B/D25-159[»]
2RTCX-ray1.50B/D25-159[»]
2RTDX-ray1.65B/D25-159[»]
2RTEX-ray1.50B/D25-159[»]
2RTFX-ray1.47B/D25-159[»]
2RTGX-ray1.39B/D25-159[»]
2RTHX-ray1.56B/D25-159[»]
2RTIX-ray1.40B/D25-159[»]
2RTJX-ray1.40A25-159[»]
2RTKX-ray1.82A25-159[»]
2RTLX-ray1.41A25-159[»]
2RTMX-ray1.30A25-159[»]
2RTNX-ray1.80B/D25-159[»]
2RTOX-ray1.58B/D25-159[»]
2RTPX-ray1.50B/D25-159[»]
2RTQX-ray1.39B/D25-159[»]
2RTRX-ray1.62B/D25-159[»]
2WPUX-ray1.92A38-183[»]
2Y3EX-ray1.45A/B37-163[»]
2Y3FX-ray1.49A37-163[»]
3MG5X-ray1.30A/B/C/D37-163[»]
3PK2X-ray1.90A38-183[»]
3RDMX-ray1.60A37-164[»]
3RDOX-ray1.40A37-164[»]
3RDQX-ray1.60A37-164[»]
3RDSX-ray1.50A37-164[»]
3RDUX-ray1.50A37-164[»]
3RDXX-ray2.10A/B37-164[»]
3RE5X-ray1.95A37-164[»]
3RE6X-ray1.82A37-164[»]
3RY1X-ray1.03A/B/C/D37-163[»]
3RY2X-ray0.95A/B37-163[»]
3T6FX-ray1.22A/B37-163[»]
3T6LX-ray1.30A37-163[»]
3WYPX-ray1.30A/B/C/D37-163[»]
3WYQX-ray1.00A/B37-163[»]
4BX5X-ray1.43A/C37-72[»]
B/D37-163[»]
4BX6X-ray1.60A/B/C/D37-163[»]
4BX7X-ray2.26A/B37-163[»]
4CPEX-ray1.06A/B37-163[»]
4CPFX-ray1.14A/B37-163[»]
4CPHX-ray1.64A/B/C/D37-163[»]
4CPIX-ray1.54A/B/C/D37-163[»]
4DNEX-ray1.88A/B1-183[»]
4EKVX-ray2.00A25-183[»]
4GD9X-ray1.50A/B/C/D37-163[»]
4GDAX-ray1.00A/B37-163[»]
4GJSX-ray1.85A/B38-183[»]
4GJVX-ray2.40A38-183[»]
4IRWX-ray1.40A36-163[»]
4JO6X-ray1.75A/B/C/D25-183[»]
4OKAX-ray2.50A38-183[»]
ProteinModelPortaliP22629.
SMRiP22629. Positions 38-159.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL1075026.

Proteomic databases

PRIDEiP22629.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP22629.

Miscellaneous databases

EvolutionaryTraceiP22629.

Family and domain databases

Gene3Di2.40.128.30. 1 hit.
InterProiIPR005469. Avidin.
IPR017889. Avidin-like_CS.
IPR005468. Avidin/str.
[Graphical view]
PfamiPF01382. Avidin. 1 hit.
[Graphical view]
PRINTSiPR00709. AVIDIN.
SUPFAMiSSF50876. SSF50876. 1 hit.
PROSITEiPS00577. AVIDIN_1. 1 hit.
PS51326. AVIDIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and nucleotide sequence of the streptavidin gene."
    Argarana C.E., Kuntz I.D., Birken S., Axel R., Cantor C.R.
    Nucleic Acids Res. 14:1871-1882(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-64.
  2. "Studies on the biotin-binding site of streptavidin. Tryptophan residues involved in the active site."
    Gitlin G., Bayer E.A., Wilchek M.
    Biochem. J. 256:279-282(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: IMPORTANCE OF TRP IN BIOTIN-BINDING.
  3. "Studies on the biotin-binding sites of avidin and streptavidin. Tyrosine residues are involved in the binding site."
    Gitlin G., Bayer E.A., Wilchek M.
    Biochem. J. 269:527-530(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: IMPORTANCE OF TYR IN BIOTIN-BINDING.
  4. "Streptavidin contains an RYD sequence which mimics the RGD receptor domain of fibronectin."
    Alon R., Bayer E.A., Wilchek M.
    Biochem. Biophys. Res. Commun. 170:1236-1241(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: CELL-BINDING.
  5. "Structural origins of high-affinity biotin binding to streptavidin."
    Weber P.C., Ohlendorf D.H., Wendoloski J.J., Salemme F.R.
    Science 243:85-88(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 37-157.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-157.
  7. "In crystals of complexes of streptavidin with peptide ligands containing the HPQ sequence the pKa of the peptide histidine is less than 3.0."
    Katz B.A., Cass R.T.
    J. Biol. Chem. 272:13220-13228(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 37-157.
  8. "Binding of biotin to streptavidin stabilizes intersubunit salt bridges between Asp61 and His87 at low pH."
    Katz B.A.
    J. Mol. Biol. 274:776-800(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 37-157.
  9. "Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex."
    Freitag S., le Trong I., Chilkoti A., Klumb L.A., Stayton P.S., Stenkamp R.E.
    J. Mol. Biol. 279:211-221(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 37-157 OF MUTANTS.

Entry informationi

Entry nameiSAV_STRAV
AccessioniPrimary (citable) accession number: P22629
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1991
Last sequence update: July 31, 1991
Last modified: March 3, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.