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3SWG

AQUIFEX AEOLICUS MurA in complex with UDP-N-acetylmuramic acid and covalent adduct of PEP with Cys124

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 Residues6
DetailsBINDING SITE FOR RESIDUE PG4 A 501
ChainResidue
AASP132
ALYS139
AVAL145
AASN350
AHOH898
AHOH928

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 A 502
ChainResidue
AGLU361
ALYS326
ATHR352
ATYR359

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PG4 A 503
ChainResidue
AGLU255
ALEU257
AARG267
AARG288
AHOH703
AHOH935

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE A 504
ChainResidue
ALYS165
APHE166
AASP167
AASN192

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 505
ChainResidue
APRO47
ATHR49
APHE231
ATHR232
AHOH901

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 506
ChainResidue
AALA323
ALYS324
AVAL363
AGLU364
AHOH845

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
AILE90
ATYR151
ATYR153

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 508
ChainResidue
AASN83

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 509
ChainResidue
AARG112
AGLY114

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 510
ChainResidue
AGLU146
AARG148
ATYR153

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 511
ChainResidue
AARG60
AARG67

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 512
ChainResidue
APHE290

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 513
ChainResidue
AASN284
AGLY285
AASN286

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 514
ChainResidue
ALYS214
ATYR221
AARG365

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 515
ChainResidue
AHIS163
AGLU191

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 516
ChainResidue
AGLU187
ALYS223
AGLN390

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 517
ChainResidue
ALEU43
AGLU45
AGLU226
AHOH701
AHOH863

site_idBC9
Number of Residues32
DetailsBINDING SITE FOR RESIDUE EPZ A 518
ChainResidue
ALYS31
AASN32
AALA101
AARG129
APRO130
AILE131
AASP132
AGLN133
ALEU168
ATHR170
AVAL171
ATHR172
ATHR310
AASP311
AILE333
APHE334
AVAL353
ALEU376
AHOH604
AHOH609
AHOH615
AHOH624
AHOH628
AHOH633
AHOH635
AHOH638
AHOH640
AHOH641
AHOH648
AHOH804
AHOH805
AHOH807

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
AQPA124

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:2YVW, ECO:0007744|PDB:3SWG
ChainResidueDetails
ALYS31

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
AARG100

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:2YVW, ECO:0007744|PDB:3SWG
ChainResidueDetails
AARG129
ATHR170
AASP311
AILE333

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
AQPA124

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PDB entries from 2025-06-18

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