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2WT4

Room temperature crystal structure of Helicobacter pylori L- asparaginase at 1.8 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0005737cellular_componentcytoplasm
A0006520biological_processamino acid metabolic process
A0006528biological_processasparagine metabolic process
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ASP A 3613
ChainResidue
AGLY15
AASN255
AGLU289
AHOH2040
AHOH2041
ATHR16
AGLY61
ASER62
AGLN63
AGLY94
ATHR95
AASP96
AALA120

Functional Information from PROSITE/UniProt
site_idPS00144
Number of Residues9
DetailsASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. LlATGGTIA
ChainResidueDetails
ALEU10-ALA18

site_idPS00917
Number of Residues11
DetailsASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GvVitHGTDTL
ChainResidueDetails
AGLY88-LEU98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: O-isoaspartyl threonine intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100
ChainResidueDetails
ATHR16

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER62
ATHR95

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
ATHR95
AASP96
ATHR16
ALYS168

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
ATHR95
ATHR16

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
AGLU289

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PDB entries from 2025-06-18

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