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9GGJ

Crystal structure of argininosuccinate lyase from Arabidopsis thaliana (AtASL) in complex with biological substrate and products - argininosuccinate, argnine and fumarate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004056molecular_functionargininosuccinate lyase activity
A0042450biological_processL-arginine biosynthetic process via ornithine
B0003824molecular_functioncatalytic activity
B0004056molecular_functionargininosuccinate lyase activity
B0042450biological_processL-arginine biosynthetic process via ornithine
C0003824molecular_functioncatalytic activity
C0004056molecular_functionargininosuccinate lyase activity
C0042450biological_processL-arginine biosynthetic process via ornithine
D0003824molecular_functioncatalytic activity
D0004056molecular_functionargininosuccinate lyase activity
D0042450biological_processL-arginine biosynthetic process via ornithine
E0003824molecular_functioncatalytic activity
E0004056molecular_functionargininosuccinate lyase activity
E0042450biological_processL-arginine biosynthetic process via ornithine
F0003824molecular_functioncatalytic activity
F0004056molecular_functionargininosuccinate lyase activity
F0042450biological_processL-arginine biosynthetic process via ornithine
G0003824molecular_functioncatalytic activity
G0004056molecular_functionargininosuccinate lyase activity
G0042450biological_processL-arginine biosynthetic process via ornithine
H0003824molecular_functioncatalytic activity
H0004056molecular_functionargininosuccinate lyase activity
H0042450biological_processL-arginine biosynthetic process via ornithine
Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsiMpQKkN
ChainResidueDetails
AGLY332-ASN341

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsBinding site: {"description":"in chain A","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"description":"in chain C","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"description":"in chain B","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsSite: {"description":"Increases basicity of active site His","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248636

PDB entries from 2026-02-04

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