Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5Y8X

Crystal structure of Bacillus licheniformis Gamma glutamyl transpeptidase with Azaserine

Functional Information from GO Data
ChainGOidnamespacecontents
A0006751biological_processglutathione catabolic process
A0036374molecular_functionglutathione hydrolase activity
B0006751biological_processglutathione catabolic process
B0036374molecular_functionglutathione hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CA A 401
ChainResidue
AASP125
AHOH657
AHOH703
AHOH742

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 402
ChainResidue
BASN455
AARG111
AARG263
ATYR264
AGLU265
AHOH574

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 403
ChainResidue
ASER132
AARG136
AHIS190
ALYS193
AHOH679
BGLN420

site_idAC4
Number of Residues5
Detailsbinding site for residue CA B 601
ChainResidue
AHIS277
AHOH667
BGLU498
BHOH733
BHOH736

site_idAC5
Number of Residues6
Detailsbinding site for residue CA B 602
ChainResidue
BGLU523
BHOH704
BHOH729
BHOH743
BHOH765
BHOH791

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO B 603
ChainResidue
BTHR518
BSER519
BTYR520
BLYS540
BGLY542
BHOH714

site_idAC7
Number of Residues12
Detailsbinding site for residue AZS B 604
ChainResidue
AARG109
BTHR399
BGLU419
BGLU438
BASP441
BSER460
BSER461
BMET462
BGLY481
BGLY482
BHOH760
BHOH819

Functional Information from PROSITE/UniProt
site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LAKTFKliRKeGSkAF
ChainResidueDetails
ALEU221-PHE236

site_idPS00462
Number of Residues25
DetailsG_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TTHfTVtdqwGNvVSyTtTIEqlFG
ChainResidueDetails
BTHR399-GLY423

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon