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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
A0006520biological_processamino acid metabolic process
A0006525biological_processarginine metabolic process
A0006526biological_processarginine biosynthetic process
A0007626biological_processlocomotory behavior
A0009791biological_processpost-embryonic development
A0016829molecular_functionlyase activity
A0019676biological_processammonia assimilation cycle
A0019752biological_processcarboxylic acid metabolic process
A0042450biological_processarginine biosynthetic process via ornithine
A0042802molecular_functionidentical protein binding
A0045429biological_processpositive regulation of nitric oxide biosynthetic process
A0070062cellular_componentextracellular exosome
B0000050biological_processurea cycle
B0003824molecular_functioncatalytic activity
B0004056molecular_functionargininosuccinate lyase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0006525biological_processarginine metabolic process
B0006526biological_processarginine biosynthetic process
B0007626biological_processlocomotory behavior
B0009791biological_processpost-embryonic development
B0016829molecular_functionlyase activity
B0019676biological_processammonia assimilation cycle
B0019752biological_processcarboxylic acid metabolic process
B0042450biological_processarginine biosynthetic process via ornithine
B0042802molecular_functionidentical protein binding
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0070062cellular_componentextracellular exosome
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P24058
ChainResidueDetails
AHIS160
BHIS160

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P24058
ChainResidueDetails
ASER281
BSER281

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: in chain A => ECO:0000250|UniProtKB:P24058
ChainResidueDetails
ASER27
BLYS329
AASN114
ATYR321
AGLN326
ALYS329
BSER27
BASN114
BTYR321
BGLN326

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: in chain C => ECO:0000250|UniProtKB:P24058
ChainResidueDetails
ATHR159
BTHR159

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: in chain B => ECO:0000250|UniProtKB:P24058
ChainResidueDetails
AASN289
BASN289

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Increases basicity of active site His => ECO:0000250|UniProtKB:P24058
ChainResidueDetails
AGLU294
BGLU294

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:Q91YI0
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q91YI0
ChainResidueDetails
ALYS7
BLYS7

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:20167786
ChainResidueDetails
ALYS69
ALYS288
BLYS69
BLYS288

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

222415

PDB entries from 2024-07-10

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