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4Q0M

Crystal structure of Pyrococcus furiosus L-asparaginase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0006520biological_processamino acid metabolic process
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 A 401
ChainResidue
AGLY10
AHOH552
AHOH578
AHOH590
ATHR11
AASP51
ASER52
AGLY82
ATHR83
AASP84
ATYR273
AHOH524

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
APRO200
ALYS201
AVAL202
AILE208
APRO209
AGLY210
ALEU211
ASER212
ATYR224

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
ATYR168
ALYS186
AASN319
AGLY322

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
AGLY134
AILE135
AARG136
AILE184
APHE187

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 4CS A 405
ChainResidue
ATYR68
AVAL192
ATHR193
ALEU194
AASN307
AASN308
AHOH595

Functional Information from PROSITE/UniProt
site_idPS00917
Number of Residues11
DetailsASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GiIvtHGTDTL
ChainResidueDetails
AGLY76-LEU86

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile; O-isoaspartyl threonine intermediate => ECO:0000305|PubMed:25478837
ChainResidueDetails
ATHR11

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:25478837
ChainResidueDetails
ATHR83
AASP84
ALYS154
ATYR273

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:25478837, ECO:0007744|PDB:4NJE, ECO:0007744|PDB:5B5U
ChainResidueDetails
ATHR11
AASP51
ASER52
ATHR83
AASP84

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PDB entries from 2024-08-07

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