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3KQJ

MurA binary complex with UDP-N-acetylglucosamine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007049biological_processcell cycle
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 GOL A 420
ChainResidue
AHIS155
APHE322
ATHR351
AHOH533
AHOH673
AHOH710

site_idAC2
Number of Residues34
DetailsBINDING SITE FOR RESIDUE UD1 A 450
ChainResidue
ATRP95
AARG120
APRO121
AVAL122
AASP123
ALEU124
AHIS125
ALYS160
ASER162
AVAL163
AGLY164
ATHR304
AASP305
AVAL327
APHE328
AARG331
APO4421
AHOH478
AHOH482
AHOH492
AHOH496
AHOH505
AHOH508
AHOH515
AHOH535
AHOH543
AHOH578
AHOH625
AHOH736
AHOH814
AHOH858
ALYS22
AASN23
AARG91

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 421
ChainResidue
ALYS22
AGLY114
ACYS115
AARG120
AARG397
AUD1450
AHOH471
AHOH543
AHOH814

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:8994972, ECO:0000305|PubMed:22378791, ECO:0007744|PDB:1UAE, ECO:0007744|PDB:3KR6
ChainResidueDetails
ACYS115

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:20392080, ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3KR6, ECO:0007744|PDB:3SWD
ChainResidueDetails
ALYS22

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0007744|PDB:3KR6
ChainResidueDetails
AVAL327
AARG91

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3KR6
ChainResidueDetails
ALYS160
AASP305
AARG120

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000305|PubMed:22378791
ChainResidueDetails
ACYS115

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PDB entries from 2024-04-17

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