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4KTM

Crystal Structure of C143S Xanthomonas campestris OleA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016746molecular_functionacyltransferase activity
A0044550biological_processsecondary metabolite biosynthetic process
A0046872molecular_functionmetal ion binding
B0005737cellular_componentcytoplasm
B0016746molecular_functionacyltransferase activity
B0044550biological_processsecondary metabolite biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG A 401
ChainResidue
AASN242
AARG245
AVAL247
AHOH568
AHOH633
AHOH687

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 402
ChainResidue
AGLY227
AHIS20
AMET21
APHE23

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 401
ChainResidue
BALA199
BTHR248
BTHR250
BVAL287

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 402
ChainResidue
BLYS102
BASP163
BHOH561
BHOH623

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 403
ChainResidue
AARG48
AGLU178
AHOH698
BARG73
BGLU312
BHIS313
BHOH641

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:22524624, ECO:0000305|PubMed:27815501, ECO:0000305|PubMed:29025976
ChainResidueDetails
AGLU117
BGLU117

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000305|PubMed:22524624, ECO:0000305|PubMed:27815501, ECO:0000305|PubMed:29025976
ChainResidueDetails
ASER143
BSER143

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22524624, ECO:0000269|PubMed:29025976, ECO:0000269|Ref.7
ChainResidueDetails
AHIS38
AASP76
BHIS38
BASP76

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for activity => ECO:0000305|PubMed:29430657
ChainResidueDetails
AHIS285
BHIS285

224931

PDB entries from 2024-09-11

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