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1XXE

RDC refined solution structure of the AaLpxC/TU-514 complex

Replaces:  1NZT
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0006629biological_processlipid metabolic process
A0006796biological_processphosphate-containing compound metabolic process
A0009245biological_processlipid A biosynthetic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019637biological_processorganophosphate metabolic process
A0046872molecular_functionmetal ion binding
A0103117molecular_functionUDP-3-O-acyl-N-acetylglucosamine deacetylase activity
A1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 319
ChainResidue
AHIS74
ATHR179
AHIS226
AASP230
ATUX320

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TUX A 320
ChainResidue
ATHR179
APHE180
ACYS181
AGLU185
AILE186
AILE189
AGLY195
AGLY198
ATYR212
ALYS227
AZN319
AHIS58
ASER59
AGLU73
AHIS74

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"},{"source":"PubMed","id":"15705580","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12819349","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15705580","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P42","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YH8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YHC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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