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Protein

Concanavalin-A

Gene
N/A
Organism
Canavalia lineata (Beach bean) (Dolichos lineatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Glucose/D-mannose specific lectin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi8ManganeseBy similarity1
Metal bindingi10CalciumBy similarity1
Metal bindingi10ManganeseBy similarity1
Metal bindingi12Calcium; via carbonyl oxygenBy similarity1
Binding sitei12CarbohydrateBy similarity1
Metal bindingi14CalciumBy similarity1
Metal bindingi19CalciumBy similarity1
Metal bindingi19ManganeseBy similarity1
Metal bindingi24ManganeseBy similarity1
Metal bindingi208CalciumBy similarity1
Binding sitei228Carbohydrate; via amide nitrogenBy similarity1

GO - Molecular functioni

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 lineata (Beach bean) (Dolichos lineatus)
Taxonomic identifieri28957 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeCanavalia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001050871 – 237Concanavalin-AAdd BLAST237

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1237
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi15 – 17Combined sources3
Beta strandi24 – 33Combined sources10
Beta strandi35 – 39Combined sources5
Beta strandi46 – 55Combined sources10
Turni56 – 59Combined sources4
Beta strandi60 – 66Combined sources7
Beta strandi72 – 78Combined sources7
Helixi81 – 83Combined sources3
Beta strandi87 – 96Combined sources10
Beta strandi98 – 100Combined sources3
Beta strandi105 – 116Combined sources12
Beta strandi124 – 132Combined sources9
Beta strandi140 – 144Combined sources5
Beta strandi150 – 152Combined sources3
Beta strandi154 – 157Combined sources4
Turni161 – 163Combined sources3
Beta strandi170 – 177Combined sources8
Beta strandi187 – 199Combined sources13
Beta strandi203 – 205Combined sources3
Beta strandi209 – 216Combined sources8
Helixi227 – 229Combined sources3
Turni230 – 232Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CWMX-ray1.95A1-237[»]
2CY6X-ray2.00A/D1-237[»]
2CYFX-ray1.80A1-237[»]
3SNMX-ray2.15A1-237[»]
4DPNX-ray2.55A/D1-237[»]
4I30X-ray1.89A1-237[»]
4TYSX-ray3.25A/B/C/D/E/F1-237[»]
4TZDX-ray3.20A/D1-237[»]
5BYNX-ray2.65A/B1-237[»]
ProteinModelPortaliP81460.
SMRiP81460.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81460.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 100Carbohydrate bindingBy similarity2

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.

P81460-1 [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 HETNALHFVF NQFSKDQKDL ILQGDATTGT
160 170 180 190 200
DGNLELTRVS SNGSPQGNSV GRALFYAPVH IWESSAVVAS FDATFTFLIK
210 220 230
SSDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN
Length:237
Mass (Da):25,497
Last modified:December 15, 1998 - v1
Checksum:i2D31C2BD3D30D66A
GO

Sequence databases

PIRiA59415.

Cross-referencesi

Sequence databases

PIRiA59415.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CWMX-ray1.95A1-237[»]
2CY6X-ray2.00A/D1-237[»]
2CYFX-ray1.80A1-237[»]
3SNMX-ray2.15A1-237[»]
4DPNX-ray2.55A/D1-237[»]
4I30X-ray1.89A1-237[»]
4TYSX-ray3.25A/B/C/D/E/F1-237[»]
4TZDX-ray3.20A/D1-237[»]
5BYNX-ray2.65A/B1-237[»]
ProteinModelPortaliP81460.
SMRiP81460.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP81460.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiCONA_CANLI
AccessioniPrimary (citable) accession number: P81460
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: November 2, 2016
This is version 88 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

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 one 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.