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6MOD

Co-Crystal structure of P. aeruginosa LpxC-50432 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0006629biological_processlipid metabolic process
A0009245biological_processlipid A biosynthetic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0103117molecular_functionUDP-3-O-acyl-N-acetylglucosamine deacetylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MG A 301
ChainResidue
AHIS78
AHIS237
AASP241
AJWV302

site_idAC2
Number of Residues18
Detailsbinding site for residue JWV A 302
ChainResidue
APHE191
AMET194
AILE197
AALA206
AGLY209
AHIS237
ALYS238
AASP241
AHIS264
AMG301
AHOH408
AHOH413
AHOH456
AHIS19
AMET62
AGLU77
AHIS78
ATHR190

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 303
ChainResidue
APHE152
AILE243
ALEU246
ATYR247
AASN251
ASER252
ALEU253

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 304
ChainResidue
ATHR60
ATHR61
AGLY263
AHIS264
AALA265
ALEU266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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