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3ZH4

crystal structure of S. pneumoniae Hungary 19A MurA1 in complex with citrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
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 Residues15
DetailsBINDING SITE FOR RESIDUE FLC A 1419
ChainResidue
ALYS22
AARG398
AHOH2030
AHOH2099
AHOH2100
AHOH2298
AHOH2336
AASN23
AARG92
ALEU118
AASP306
AARG332
AASP370
ALEU371
AARG372

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 1420
ChainResidue
AARG92
ASER164
AVAL165
AGLY166
ATYR329
AHOH2102
AHOH2348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
ACYS116

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A749
ChainResidueDetails
AARG121
AASP306
AILE328
ALYS22
AARG92

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
ACYS116

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PDB entries from 2024-06-12

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