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1EJC

Crystal structure of unliganded mura (type2)

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 Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 701
ChainResidue
AMET1
AASP2
ATYR393
AHOH502
AHOH731

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
AHOH694
AHOH706
AHOH809
AARG252
ATRP279
AARG340
AGLY362

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
AHIS344
AHIS355
AGLY356
AHOH733
AHOH819
AHOH935

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 603
ChainResidue
AARG91
AALA92
AILE94
ATRP95
AHIS125
AGLY164
AHOH508
AHOH764
AHOH847
AHOH905

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 604
ChainResidue
APHE104
AASN330
APHE332
AMET333
APRO336
AHOH455
AHOH838
AHOH920

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
AARG91

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_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1uae
ChainResidueDetails
AASP305
AARG397
ACYS115
AASN23

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

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PDB entries from 2024-07-24

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