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2WLT

The crystal structure of Helicobacter pylori L-asparaginase at 1.4 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 Residues14
DetailsBINDING SITE FOR RESIDUE ASP A 1333
ChainResidue
AGLY15
AALA120
AASN255
AGLU289
AHOH2107
AHOH2137
ATHR16
ASER31
AGLY61
ASER62
AGLN63
AGLY94
ATHR95
AASP96

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 Residues5
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
ATHR95
ATHR16
AASP96
ATYR29
ALYS168

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
ATHR95
ATHR16
ATYR29

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

223166

PDB entries from 2024-07-31

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