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1NAW

ENOLPYRUVYL TRANSFERASE

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
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0008360biological_processregulation of cell shape
B0008760molecular_functionUDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0019277biological_processUDP-N-acetylgalactosamine biosynthetic process
B0051301biological_processcell division
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HAI A 479
ChainResidue
AVAL250
AGLU274
ATRP279
AHAI480
BLYS248
BGLU274
BTRP279

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HAI A 480
ChainResidue
AHAI479
BVAL250
BTRP279
AVAL250
ATRP279

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH
ChainResidueDetails
ACYS115
BCYS115

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ
ChainResidueDetails
ALYS22
BLYS22

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
AARG91
BARG91

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH, ECO:0007744|PDB:3SWQ
ChainResidueDetails
AARG120
AASP305
AILE327
BARG120
BASP305
BILE327

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ
ChainResidueDetails
ALYS160
BLYS160

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269|PubMed:22378791
ChainResidueDetails
ACYS115
BCYS115

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1uae
ChainResidueDetails
AASP305
AARG397
ACYS115
AASN23

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1uae
ChainResidueDetails
BASP305
BARG397
BCYS115
BASN23

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

site_idMCSA2
Number of Residues6
DetailsM-CSA 369
ChainResidueDetails
BLYS22electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
BASN23electrostatic stabiliser, hydrogen bond donor
BCYS115activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
BARG120electrostatic stabiliser, proton acceptor, proton donor
BASP305activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BARG397electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-07-24

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