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

2RL2

Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0007049biological_processcell cycle
A0008360biological_processregulation of cell shape
A0008760molecular_functionUDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0019277biological_processUDP-N-acetylgalactosamine biosynthetic process
A0051301biological_processcell division
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 713
ChainResidue
ALYS22
AARG93
AARG122
AARG399
AHOH781
AHOH831

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 714
ChainResidue
ALYS146
AGLN110
AGLU142
ATYR144

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 715
ChainResidue
AARG157
AARG269
AHOH887

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GG6 A 425
ChainResidue
ACYS117
ASER118
AILE119
AHOH872
AHOH882
AHOH958

site_idAC5
Number of Residues27
DetailsBINDING SITE FOR RESIDUE UD1 A 712
ChainResidue
AASN23
AARG93
ATRP97
AALA121
AARG122
APRO123
AASP125
ALEU126
AHIS127
ALYS162
ASER164
AGLY166
ATHR306
AASP307
AILE329
APHE330
AARG333
AHOH717
AHOH718
AHOH743
AHOH776
AHOH777
AHOH781
AHOH799
AHOH809
AHOH934
AHOH948

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00111, ECO:0000305|PubMed:22378791
ChainResidueDetails
ACYS117

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWE
ChainResidueDetails
ALYS22

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
AARG93

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWE
ChainResidueDetails
AARG122
ASER164
AASP307
AILE329

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111, ECO:0000305|PubMed:22378791
ChainResidueDetails
ACYS117

217705

PDB entries from 2024-03-27

PDB statisticsPDBj update infoContact PDBjnumon