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

4S12

1.55 Angstrom Crystal Structure of N-acetylmuramic acid 6-phosphate Etherase from Yersinia enterocolitica.

Functional Information from GO Data
ChainGOidnamespacecontents
A0006040biological_processamino sugar metabolic process
A0009254biological_processpeptidoglycan turnover
A0016803molecular_functionether hydrolase activity
A0016829molecular_functionlyase activity
A0016835molecular_functioncarbon-oxygen lyase activity
A0046348biological_processamino sugar catabolic process
A0097173biological_processN-acetylmuramic acid catabolic process
A0097175biological_process1,6-anhydro-N-acetyl-beta-muramic acid catabolic process
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
B0006040biological_processamino sugar metabolic process
B0009254biological_processpeptidoglycan turnover
B0016803molecular_functionether hydrolase activity
B0016829molecular_functionlyase activity
B0016835molecular_functioncarbon-oxygen lyase activity
B0046348biological_processamino sugar catabolic process
B0097173biological_processN-acetylmuramic acid catabolic process
B0097175biological_process1,6-anhydro-N-acetyl-beta-muramic acid catabolic process
B0097367molecular_functioncarbohydrate derivative binding
B1901135biological_processcarbohydrate derivative metabolic process
C0006040biological_processamino sugar metabolic process
C0009254biological_processpeptidoglycan turnover
C0016803molecular_functionether hydrolase activity
C0016829molecular_functionlyase activity
C0016835molecular_functioncarbon-oxygen lyase activity
C0046348biological_processamino sugar catabolic process
C0097173biological_processN-acetylmuramic acid catabolic process
C0097175biological_process1,6-anhydro-N-acetyl-beta-muramic acid catabolic process
C0097367molecular_functioncarbohydrate derivative binding
C1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ASER73
AHOH471
AHOH587
AALA139
AALA140
ASER141
ATHR144
ALYS233
AHOH407
AHOH436
AHOH449

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AARG94
ALYS218
AHOH564
AHOH572

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AARG143
AHOH462
AHOH603
AHOH628
AHOH701
AHOH760

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AHIS287
AALA293
AHOH477
AHOH537

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
BSER73
BALA139
BALA140
BSER141
BTHR144
BHOH425
BHOH501
BHOH549
BHOH695

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BPRO86
BHIS92
BHOH495
BHOH504
BHOH676
CLYS108
CALA109

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 301
ChainResidue
CARG237
CARG240

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 302
ChainResidue
CGLY89
CVAL90
CPRO91
CARG94
CLYS218
CHOH685

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 303
ChainResidue
AARG122
CHIS287
CHOH588

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG C 304
ChainResidue
BHOH640
CASP19
CTHR20
CLEU21
CHOH664

Functional Information from PROSITE/UniProt
site_idPS01272
Number of Residues18
DetailsGCKR Glucokinase regulatory protein family signature. GPEaLTGSTRMKSGTaqK
ChainResidueDetails
AGLY185-LYS202

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon