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1YH8

Crystal structure of Aquifex aeolicus LpxC deacetylase complexed with palmitate

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
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0006629biological_processlipid metabolic process
B0006796biological_processphosphate-containing compound metabolic process
B0009245biological_processlipid A biosynthetic process
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0019637biological_processorganophosphate metabolic process
B0046872molecular_functionmetal ion binding
B0103117molecular_functionUDP-3-O-acyl-N-acetylglucosamine deacetylase activity
B1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHIS79
AHIS238
AASP242
APAM801

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
AHIS58
AHIS200

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 504
ChainResidue
BGLY2
BGLU126
AILE27
AHIS29
AGLU95

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 505
ChainResidue
BHIS79
BHIS238
BASP242
BPAM802

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 507
ChainResidue
BHIS58
BHIS200
BCL603
BHOH863

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 601
ChainResidue
AHIS79
AILE103
ASER107

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 602
ChainResidue
BGLY15
BVAL16
BILE103
BLEU104

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 603
ChainResidue
BHIS58
BHIS200
BZN507

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PAM A 801
ChainResidue
AILE18
AHIS58
AGLU78
AHIS79
ATHR191
AGLY210
AHIS238
AASP242
AHIS265
AZN501

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PAM B 802
ChainResidue
ALEU212
BILE18
BHIS58
BGLU78
BHIS79
BTHR191
BSER211
BHIS238
BASP242
BHIS265
BZN505

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

site_idSWS_FT_FI2
Number of Residues6
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

249697

PDB entries from 2026-02-25

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