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1HFW

X-ray structure of the complex between Erwinia chrysanthemi L-asparaginase and L-Glutamate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0006520biological_processamino acid metabolic process
A0006528biological_processasparagine metabolic process
A0016787molecular_functionhydrolase activity
B0004067molecular_functionasparaginase activity
B0006520biological_processamino acid metabolic process
B0006528biological_processasparagine metabolic process
B0016787molecular_functionhydrolase activity
C0004067molecular_functionasparaginase activity
C0006520biological_processamino acid metabolic process
C0006528biological_processasparagine metabolic process
C0016787molecular_functionhydrolase activity
D0004067molecular_functionasparaginase activity
D0006520biological_processamino acid metabolic process
D0006528biological_processasparagine metabolic process
D0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLU A 350
ChainResidue
AGLY14
AHOH2215
AHOH2216
CSER254
ATHR15
AALA61
ASER62
AGLU63
AGLY94
ATHR95
AASP96
AALA120

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLU B 350
ChainResidue
BGLY14
BTHR15
BALA61
BSER62
BGLU63
BGLY94
BTHR95
BASP96
BHOH2249
BHOH2250
BHOH2251
DSER254

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU C 350
ChainResidue
ASER254
CGLY14
CTHR15
CALA61
CSER62
CGLU63
CGLY94
CTHR95
CASP96
CALA120
CHOH2022
CHOH2233
CHOH2235

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLU D 350
ChainResidue
BSER254
DGLY14
DTHR15
DALA61
DSER62
DGLU63
DGLY94
DTHR95
DASP96
DHOH2257
DHOH2258
DHOH2259

Functional Information from PROSITE/UniProt
site_idPS00144
Number of Residues9
DetailsASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IlATGGTIA
ChainResidueDetails
AILE9-ALA17

site_idPS00917
Number of Residues11
DetailsASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GvVitHGTDTV
ChainResidueDetails
AGLY88-VAL98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: O-isoaspartyl threonine intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:11755201, ECO:0000269|PubMed:8348975
ChainResidueDetails
ATHR15
BTHR15
CTHR15
DTHR15

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ASER62
ATHR95
BSER62
BTHR95
CSER62
CTHR95
DSER62
DTHR95

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
ATHR15
ATHR95
AASP96
ALYS168

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
BTHR15
BTHR95
BASP96
BLYS168

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
CTHR15
CTHR95
CASP96
CLYS168

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
DTHR15
DTHR95
DASP96
DLYS168

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
AVAL284
CTHR15
CTHR95

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
DTHR15
DTHR95
BVAL284

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
ATHR15
ATHR95
CVAL284

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
DVAL284
BTHR15
BTHR95

226707

PDB entries from 2024-10-30

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