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1XWO

crystal structrue of goose delta crystallin

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004056molecular_functionargininosuccinate lyase activity
A0005212molecular_functionstructural constituent of eye lens
A0005829cellular_componentcytosol
A0006526biological_processL-arginine biosynthetic process
A0008652biological_processamino acid biosynthetic process
A0016829molecular_functionlyase activity
A0042450biological_processL-arginine biosynthetic process via ornithine
B0003824molecular_functioncatalytic activity
B0004056molecular_functionargininosuccinate lyase activity
B0005212molecular_functionstructural constituent of eye lens
B0005829cellular_componentcytosol
B0006526biological_processL-arginine biosynthetic process
B0008652biological_processamino acid biosynthetic process
B0016829molecular_functionlyase activity
B0042450biological_processL-arginine biosynthetic process via ornithine
C0003824molecular_functioncatalytic activity
C0004056molecular_functionargininosuccinate lyase activity
C0005212molecular_functionstructural constituent of eye lens
C0005829cellular_componentcytosol
C0006526biological_processL-arginine biosynthetic process
C0008652biological_processamino acid biosynthetic process
C0016829molecular_functionlyase activity
C0042450biological_processL-arginine biosynthetic process via ornithine
D0003824molecular_functioncatalytic activity
D0004056molecular_functionargininosuccinate lyase activity
D0005212molecular_functionstructural constituent of eye lens
D0005829cellular_componentcytosol
D0006526biological_processL-arginine biosynthetic process
D0008652biological_processamino acid biosynthetic process
D0016829molecular_functionlyase activity
D0042450biological_processL-arginine biosynthetic process via ornithine
Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSslMpQKkN
ChainResidueDetails
AGLY280-ASN289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"description":"in chain A","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"description":"in chain C","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"description":"in chain B","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Increases basicity of active site His","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
AHIS160
ATHR159
BSER281
BLYS287
BGLU294

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
ASER281
ALYS287
AGLU294
BHIS160
BTHR159

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
CHIS160
CTHR159
DSER281
DLYS287
DGLU294

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
CSER281
CLYS287
CGLU294
DHIS160
DTHR159

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PDB entries from 2026-01-21

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