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1DQ2

Unlocked metal-free concanavalin A

Functional Information from GO Data
ChainGOidnamespacecontents
A0005537molecular_functionD-mannose binding
A0030246molecular_functioncarbohydrate binding
A0035821biological_processmodulation of process of another organism
A0046872molecular_functionmetal ion binding
A0090729molecular_functiontoxin activity
B0005537molecular_functionD-mannose binding
B0030246molecular_functioncarbohydrate binding
B0035821biological_processmodulation of process of another organism
B0046872molecular_functionmetal ion binding
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 241
ChainResidue
APHE130
AGLN137
AASP139
BASN124

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 242
ChainResidue
AASN124
AALA125
BPHE130
BGLN137
BASP139

Functional Information from PROSITE/UniProt
site_idPS00307
Number of Residues7
DetailsLECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVELDT
ChainResidueDetails
AVAL5-THR11

site_idPS00308
Number of Residues10
DetailsLECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPEWVRVGLS
ChainResidueDetails
ALEU85-SER94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING:
ChainResidueDetails
AGLU8
BTYR12
BASN14
BASP19
BHIS24
BLEU99
AASP10
ATYR12
AASN14
AASP19
AHIS24
ALEU99
BGLU8
BASP10

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER34
AASP208
BSER34
BASP208

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10506175
ChainResidueDetails
AARG228
BARG228

222624

PDB entries from 2024-07-17

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