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1P42

Crystal structure of Aquifex aeolicus LpxC Deacetylase (Zinc-Inhibited Form)

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHIS79
AHIS238
AASP242
AZN502
AHOH602

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AHOH602
AGLU78
AHIS265
AZN501
AMYR601

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
AHIS58
AHIS200
AHOH603
AHOH604

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 504
ChainResidue
AGLY2
AGLU126
BILE27
BHIS29
BGLU95

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 505
ChainResidue
BHIS79
BHIS238
BASP242
BZN506
BHOH603

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 506
ChainResidue
BGLU78
BHIS265
BZN505
BMYR602
BHOH603

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 507
ChainResidue
BHIS58
BHIS200
BHOH604
BHOH605

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MYR A 601
ChainResidue
AHIS58
AGLU78
ATHR191
AILE201
AGLY207
AHIS265
AZN502
AHOH633
AHOH732

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MYR B 602
ChainResidue
BHIS58
BSER59
BGLU78
BTHR191
BILE201
BGLY207
BHIS265
BZN506
BHOH603
BHOH624
BHOH734

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

246704

PDB entries from 2025-12-24

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