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3NTX

Crystal Structure of L-asparaginase I from Yersinia pestis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0004067molecular_functionasparaginase activity
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GOL A 341
ChainResidue
APRO175
AHOH447
AHOH475
AHOH494
AHOH501
AASN176
ATHR271
ACYS273
AILE274
AASP299
AMSE300
ATHR301
AVAL302

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 343
ChainResidue
AGLN232
AILE265
AHOH432

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 341
ChainResidue
BGLN232
BVAL234
BHOH457

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 342
ChainResidue
APRO56
BGLN76
BTYR79
BASP80
BHOH389
BHOH539
BHOH584

Functional Information from PROSITE/UniProt
site_idPS00144
Number of Residues9
DetailsASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. VaYTGGTIG
ChainResidueDetails
AVAL8-GLY16

site_idPS00917
Number of Residues11
DetailsASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GfVilHGTDTM
ChainResidueDetails
AGLY84-MSE94

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PDB entries from 2024-10-09

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