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1DJO

Crystal structure of Pseudomonas 7A Glutaminase-asparaginase with the inhibitor donv covalently bound in the active site

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0004359molecular_functionglutaminase activity
A0006520biological_processamino acid metabolic process
A0006528biological_processasparagine metabolic process
A0016787molecular_functionhydrolase activity
A0042597cellular_componentperiplasmic space
A0050417molecular_functionglutamin-(asparagin-)ase activity
B0004067molecular_functionasparaginase activity
B0004359molecular_functionglutaminase activity
B0006520biological_processamino acid metabolic process
B0006528biological_processasparagine metabolic process
B0016787molecular_functionhydrolase activity
B0042597cellular_componentperiplasmic space
B0050417molecular_functionglutamin-(asparagin-)ase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CAB B 4000
ChainResidue
AGLU1294
BTHR3100
BASP3101
BSER3125
BGLY3019
BTHR3020
BTYR3034
BALA3036
BALA3066
BSER3067
BGLU3068
BGLY3099

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CAB A 4001
ChainResidue
AGLY1019
ATHR1020
ATYR1034
AALA1066
ASER1067
AGLU1068
AGLY1099
ATHR1100
AASP1101
ASER1125
BGLU3294

Functional Information from PROSITE/UniProt
site_idPS00144
Number of Residues9
DetailsASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IlATGGTIA
ChainResidueDetails
AILE1014-ALA1022

site_idPS00917
Number of Residues11
DetailsASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GiVitHGTDTL
ChainResidueDetails
AGLY1093-LEU1103

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:10684596
ChainResidueDetails
ATHR1020
BTHR3020

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER1067
ATHR1100
BSER3067
BTHR3100

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 10684596
ChainResidueDetails
ATHR1020
ATYR1034
ATHR1100
BGLU3294

site_idCSA2
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 10684596
ChainResidueDetails
AGLU1294
BTHR3020
BTHR3100
BTYR3034

site_idMCSA1
Number of Residues6
DetailsM-CSA 29
ChainResidueDetails
ATHR1020covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
ATYR1034hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ATHR1100hydrogen bond acceptor, hydrogen bond donor
AASP1101hydrogen bond acceptor
ALYS1173hydrogen bond acceptor, hydrogen bond donor
AGLU1294hydrogen bond acceptor, proton acceptor, proton donor, proton relay

site_idMCSA2
Number of Residues6
DetailsM-CSA 29
ChainResidueDetails
BTHR3020covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BTYR3034hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
BTHR3100hydrogen bond acceptor, hydrogen bond donor
BASP3101hydrogen bond acceptor
BLYS3173hydrogen bond acceptor, hydrogen bond donor
BGLU3294hydrogen bond acceptor, proton acceptor, proton donor, proton relay

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PDB entries from 2024-11-06

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