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1DLG

CRYSTAL STRUCTURE OF THE C115S ENTEROBACTER CLOACAE MURA IN THE UN-LIGANDED STATE

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 Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 1500
ChainResidue
AGLU135
ALYS137
ALYS144
AHAI1424

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 1501
ChainResidue
BHAI1420
AARG252
AASP278
AHOH658
BARG252
BASN253

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 1502
ChainResidue
AARG401
AGLU403
AASP404
AARG407
AARG415
AHOH695
AHOH917
AHOH984

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 1503
ChainResidue
ASER162
AVAL163
AGLY164
AHOH460
AHOH749

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 1504
ChainResidue
BASN23
BASP305
BARG371
BHOH454
BHOH728
BHOH980

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 1506
ChainResidue
AGLY118
AALA119
BALA119
BASP159
BLYS160
BHOH1082

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 1507
ChainResidue
BALA92
BTRP95
BHOH520

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 1508
ChainResidue
BGLY319
BTHR320
BHIS355
BHOH589

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 1509
ChainResidue
AHOH887
BTYR393
BHIS394
BARG397
BHOH477
BHOH891

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HAI B 1420
ChainResidue
AVAL250
ATRP279
BTRP279
BHOH552
BPO41501

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HAI B 1422
ChainResidue
AVAL250
AGLU274
ASER281
BVAL250
BGLU274
BSER281

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HAI A 1424
ChainResidue
APHE80
AGLU135
ALYS144
AASN148
APO41500

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
ASER115
BSER115

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
ASER115
BSER115

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1uae
ChainResidueDetails
AASP305
AARG397
ASER115
AASN23

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1uae
ChainResidueDetails
BASP305
BARG397
BSER115
BASN23

site_idMCSA1
Number of Residues6
DetailsM-CSA 369
ChainResidueDetails
ALYS22electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
AASN23electrostatic stabiliser, hydrogen bond donor
ASER115activator, 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
BSER115activator, 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 2024-09-18

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