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1XXE

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

Replaces:  1NZT
Functional Information from GO Data
ChainGOidnamespacecontents
A0006796biological_processphosphate-containing compound metabolic process
A0008759molecular_functionUDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity
A0009245biological_processlipid A biosynthetic process
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
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000305|PubMed:15705580
ChainResidueDetails
AHIS253

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:12819349, ECO:0000269|PubMed:15705580, ECO:0007744|PDB:1P42, ECO:0007744|PDB:1YH8, ECO:0007744|PDB:1YHC
ChainResidueDetails
AHIS74
AHIS226
AASP230

222036

PDB entries from 2024-07-03

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