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3NXK

Crystal Structure of Probable Cytoplasmic L-asparaginase from Campylobacter jejuni

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
E0004067molecular_functionasparaginase activity
E0006520biological_processamino acid metabolic process
E0006528biological_processasparagine metabolic process
E0016787molecular_functionhydrolase activity
F0004067molecular_functionasparaginase activity
F0006520biological_processamino acid metabolic process
F0006528biological_processasparagine metabolic process
F0016787molecular_functionhydrolase activity
G0004067molecular_functionasparaginase activity
G0006520biological_processamino acid metabolic process
G0006528biological_processasparagine metabolic process
G0016787molecular_functionhydrolase activity
H0004067molecular_functionasparaginase activity
H0006520biological_processamino acid metabolic process
H0006528biological_processasparagine metabolic process
H0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 341
ChainResidue
AGLY15
ATHR16
AASP62
ASER63
AGLY94
ATHR95
AASP96
AHOH873

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 342
ChainResidue
AASP112
ALYS113
ALYS205
AHOH899
ASER111

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 343
ChainResidue
ATHR318
ASER319
FLYS213

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 344
ChainResidue
AASN144
AGLY191
ALYS192
AVAL193
APHE194

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 341
ChainResidue
BGLY15
BTHR16
BASP62
BSER63
BGLY94
BTHR95
BASP96

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 342
ChainResidue
BSER111
BASP112
BLYS113
BLYS205

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 343
ChainResidue
BTYR327
BLYS330
BTYR331

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 344
ChainResidue
BILE256
BLYS261
BASP262
BLYS265
BHOH697
CASN65

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 345
ChainResidue
BGLU292
BLYS322
BGLN325
BGLU326
BLEU329
BHOH365

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 C 341
ChainResidue
CGLY15
CTHR16
CASP62
CSER63
CGLY94
CTHR95
CASP96
CHOH387
CHOH823

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 342
ChainResidue
CSER111
CASP112
CLYS205

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL C 343
ChainResidue
CTHR318
CSER319

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY C 344
ChainResidue
ATYR196
CLYS201
CCYS284
CGLU300
CASP301

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 D 341
ChainResidue
DGLY15
DTHR16
DASP62
DSER63
DGLY94
DTHR95
DASP96
DHOH358
DHOH800

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 342
ChainResidue
DSER111
DASP112
DHOH1038

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL D 343
ChainResidue
DTHR318
DSER319
DASP320

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL D 344
ChainResidue
DLYS261
DLYS265
DASP291

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 E 341
ChainResidue
EGLY15
ETHR16
EASP62
ESER63
EGLY94
ETHR95
EASP96

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 E 342
ChainResidue
ESER111
EASP112
ELYS205

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL E 343
ChainResidue
EILE256
ELYS258
ELYS261
ELYS265
HASN65

site_idCC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL E 344
ChainResidue
ELYS236
ELYS270

site_idCC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL E 332
ChainResidue
EARG122
ESER128
EASP130
EASN157
EVAL174
EHOH1028
FARG122
FSER128
FALA129
FHOH406

site_idCC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 F 341
ChainResidue
FGLY15
FTHR16
FSER63
FGLY94
FTHR95
FASP96
FHOH973

site_idCC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 F 342
ChainResidue
FSER111
FASP112
FLYS113
FLYS205

site_idCC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY F 343
ChainResidue
ALYS213
FTHR318
FSER319

site_idCC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 G 341
ChainResidue
GGLY15
GTHR16
GSER63
GGLY94
GTHR95
GASP96
GHOH872

site_idCC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 G 342
ChainResidue
GSER111
GASP112
GLYS113

site_idDC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 H 341
ChainResidue
HGLY15
HTHR16
HASP62
HSER63
HGLY94
HTHR95
HASP96

site_idDC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 H 342
ChainResidue
HSER111
HASP112
HLYS113
HLYS205

Functional Information from PROSITE/UniProt
site_idPS00144
Number of Residues9
DetailsASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IlGTGGTIA
ChainResidueDetails
AILE10-ALA18

site_idPS00917
Number of Residues11
DetailsASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GvVitHGTDTM
ChainResidueDetails
AGLY88-MSE98

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PDB entries from 2024-07-31

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