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7CI6

Crystal structure of P.aeruginosa LpxC in complex with inhibitor

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
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0006629biological_processlipid metabolic process
B0009245biological_processlipid A biosynthetic process
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0103117molecular_functionUDP-3-O-acyl-N-acetylglucosamine deacetylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue FY6 A 1300
ChainResidue
AMET62
AZN1301
AGLU77
AHIS78
ATHR190
APHE191
ALEU200
AALA206
AHIS237
AASP241

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1301
ChainResidue
AHIS78
AHIS237
AASP241
AFY61300

site_idAC3
Number of Residues12
Detailsbinding site for residue FY6 B 1300
ChainResidue
BLEU18
BMET62
BGLU77
BHIS78
BTHR190
BPHE191
BALA206
BHIS237
BASP241
BHIS264
BZN1301
BHOH1423

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 1301
ChainResidue
BHIS78
BHIS237
BASP241
BFY61300

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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