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6DUI

Crystal structure of LpxC from Pseudomonas aeruginosa in complex with PT801

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
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 Residues20
Detailsbinding site for residue HAY A 401
ChainResidue
ALEU18
AMET194
AVAL216
AHIS237
ALYS238
AASP241
AHIS264
AJ1M402
AZN403
AHOH570
AHOH628
AHIS19
AHOH675
AMET62
AGLU77
AHIS78
ATHR190
APHE191
AGLY192
APHE193

site_idAC2
Number of Residues17
Detailsbinding site for residue J1M A 402
ChainResidue
AMET62
ASER63
AGLU77
AHIS78
ATHR190
APHE191
AGLY192
AMET194
AARG201
AGLY209
AHIS237
AASP241
AHIS264
AHAY401
AZN403
AHOH504
AHOH570

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN A 403
ChainResidue
AHIS78
AHIS237
AASP241
AHAY401
AJ1M402

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 404
ChainResidue
AGLY263
ALEU266

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 405
ChainResidue
ATYR230
AGLU231
AASP232
ALYS236

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO A 406
ChainResidue
AMET1
AGLU225
ATHR285
AGLU287
AHOH554
AHOH556

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

246704

PDB entries from 2025-12-24

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