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1K62

Crystal Structure of the Human Argininosuccinate Lyase Q286R Mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0003824molecular_functioncatalytic activity
A0004056molecular_functionargininosuccinate lyase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006525biological_processarginine metabolic process
A0006526biological_processL-arginine biosynthetic process
A0008652biological_processamino acid biosynthetic process
A0016829molecular_functionlyase activity
A0042450biological_processL-arginine biosynthetic process via ornithine
A0042802molecular_functionidentical protein binding
A0045429biological_processpositive regulation of nitric oxide biosynthetic process
A0070062cellular_componentextracellular exosome
A0170033biological_processL-amino acid metabolic process
B0000050biological_processurea cycle
B0003824molecular_functioncatalytic activity
B0004056molecular_functionargininosuccinate lyase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006525biological_processarginine metabolic process
B0006526biological_processL-arginine biosynthetic process
B0008652biological_processamino acid biosynthetic process
B0016829molecular_functionlyase activity
B0042450biological_processL-arginine biosynthetic process via ornithine
B0042802molecular_functionidentical protein binding
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0070062cellular_componentextracellular exosome
B0170033biological_processL-amino acid metabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"description":"in chain A","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"description":"in chain C","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"description":"in chain B","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Increases basicity of active site His","evidences":[{"source":"UniProtKB","id":"P24058","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"20167786","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91YI0","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

246031

PDB entries from 2025-12-10

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