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P81461

- CONA_CANCT

UniProt

P81461 - CONA_CANCT

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Protein

Concanavalin-A

Gene
N/A
Organism
Canavalia cathartica (Jackbean) (Canavalia virosa)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Glucose/D-mannose specific lectin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Manganese
Metal bindingi10 – 101Calcium1 Publication
Metal bindingi10 – 101Manganese
Metal bindingi12 – 121Calcium; via carbonyl oxygen1 Publication
Binding sitei12 – 121CarbohydrateBy similarity
Metal bindingi14 – 141Calcium1 Publication
Metal bindingi19 – 191Calcium1 Publication
Metal bindingi19 – 191Manganese
Metal bindingi24 – 241Manganese
Metal bindingi208 – 2081CalciumBy similarity
Binding sitei228 – 2281Carbohydrate; via amide nitrogenBy similarity

GO - Molecular functioni

  1. mannose binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin, Manganese, Mannose-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Concanavalin-A
Short name:
Con A
OrganismiCanavalia cathartica (Jackbean) (Canavalia virosa)
Taxonomic identifieri28958 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeCanavalia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 237237Concanavalin-APRO_0000105088Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
237
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi15 – 173Combined sources
Beta strandi24 – 3310Combined sources
Beta strandi35 – 395Combined sources
Beta strandi46 – 5510Combined sources
Turni56 – 594Combined sources
Beta strandi60 – 667Combined sources
Beta strandi73 – 786Combined sources
Helixi81 – 833Combined sources
Beta strandi87 – 9610Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi105 – 11814Combined sources
Beta strandi123 – 13210Combined sources
Beta strandi140 – 1445Combined sources
Helixi150 – 1523Combined sources
Beta strandi153 – 1575Combined sources
Beta strandi170 – 1778Combined sources
Beta strandi186 – 19813Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi209 – 2157Combined sources
Helixi227 – 2293Combined sources
Turni230 – 2323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A7AX-ray1.75A1-237[»]
2G4IX-ray2.40A1-237[»]
3QLQX-ray1.70A/B/C/D1-237[»]
ProteinModelPortaliP81461.
SMRiP81461. Positions 1-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81461.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1002Carbohydrate bindingBy similarity

Sequence similaritiesi

Belongs to the leguminous lectin family.Curated

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P81461-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
ADTIVAVELD TYPNTDIGDP SYPHIGIDIK SVRSKKTAKW NMQNGKVGTA
60 70 80 90 100
HIIYNSVGKR LSAVVSYPNG DSATVSYDVD LDNVLPEWVR VGLSASTGLY
110 120 130 140 150
KETNTILSWS FTSKLKSNST HETNALHFMF NQFSKDQKDL ILQGDATTGT
160 170 180 190 200
DGNLELTRVS SNGSPQGNSV GRALFYAPVH IWESSAVVAS FDATFTFLIK
210 220 230
SPDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN
Length:237
Mass (Da):25,539
Last modified:December 15, 1998 - v1
Checksum:iDD31D2BFCC6EDD07
GO

Sequence databases

PIRiA59417.

Cross-referencesi

Sequence databases

PIRi A59417.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2A7A X-ray 1.75 A 1-237 [» ]
2G4I X-ray 2.40 A 1-237 [» ]
3QLQ X-ray 1.70 A/B/C/D 1-237 [» ]
ProteinModelPortali P81461.
SMRi P81461. Positions 1-237.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P81461.

Family and domain databases

Gene3Di 2.60.120.200. 2 hits.
InterProi IPR013320. ConA-like_dom.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view ]
Pfami PF00139. Lectin_legB. 2 hits.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Primary structures of concanavalin A-like lectins from seeds of two species of Canavalia."
    Fujimura S., Terada S., Jayavardhanan K.K., Panikkar K.R., Kimoto E.
    Phytochemistry 33:985-987(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths."
    Mueller-Dieckmann C., Panjikar S., Schmidt A., Mueller S., Kuper J., Geerlof A., Wilmanns M., Singh R.K., Tucker P.A., Weiss M.S.
    Acta Crystallogr. D 63:366-380(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH CALCIUM AND MANGANESE IONS.

Entry informationi

Entry nameiCONA_CANCT
AccessioniPrimary (citable) accession number: P81461
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: November 26, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds one manganese (or another transition metal) ion and one calcium ion. The metal ions are essential for the saccharide-binding and cell-agglutinating activities.

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