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

4EII

Unliganded E. cloacae R91K MurA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
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 Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AARG252
ATRP279
AARG340
AGLY362
AALA363
AHOH668
AHOH841
AHOH982

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
AHIS355
AGLY356
AHOH671
AHOH703
AHOH1010
AHOH1064
AHIS344

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AARG187
ATHR210
AASP211
AHOH862
AHOH1030
AHOH1037

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
ATHR10
AASN412

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
AGLN59
AGLY61
AASN79

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
AARG227
AASN253
AHOH938
AHOH987

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
AGLU37
ALYS91
ALEU221
AGLY222
AHOH1034

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 508
ChainResidue
ATRP95
AHOH837

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 509
ChainResidue
AARG220
APHE328
AARG331
AASP369
AHOH891

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGE A 510
ChainResidue
AASN196
ATYR226
AARG227
AHOH624
AHOH785
AHOH910
AHOH1057

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH
ChainResidueDetails
ACYS115

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

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
ALYS91

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH, ECO:0007744|PDB:3SWQ
ChainResidueDetails
AARG120
AASP305
AILE327

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ
ChainResidueDetails
ALYS160

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269|PubMed:22378791
ChainResidueDetails
ACYS115

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 369
ChainResidueDetails
ALYS22electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
AASN23electrostatic stabiliser, hydrogen bond donor
ACYS115activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
AARG120electrostatic stabiliser, proton acceptor, proton donor
AASP305activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG397electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon