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3UHM

UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase 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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 300
ChainResidue
AHIS78
AHIS237
AASP241
ARFN303

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE RFN A 303
ChainResidue
ATHR190
APHE191
AGLY192
ALEU200
AHIS237
ALYS238
AASP241
AHIS264
AZN300
AEDO302
AHOH375
ALEU18
AHIS19
AMET62
AGLU77
AHIS78

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GAI A 301
ChainResidue
ALEU205
AALA206
AHOH470

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AMET62
APHE191
AGLY192
APHE193
AASP196
ARFN303

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"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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