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5BUX

Crystal Structure of 3-hydroxyacyl-ACP dehydratase (FabZ) from Yersinia pestis with glycerol bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006633biological_processfatty acid biosynthetic process
A0009245biological_processlipid A biosynthetic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0019171molecular_function(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity
B0005737cellular_componentcytoplasm
B0006633biological_processfatty acid biosynthetic process
B0009245biological_processlipid A biosynthetic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0019171molecular_function(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 201
ChainResidue
AHIS19
AGLU68
AHOH309
AHOH317
AHOH386
BHIS54

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 202
ChainResidue
BHIS19
BGLU68
BHOH324
AHIS54
AGLY63
AHOH326

site_idAC3
Number of Residues5
Detailsbinding site for residue SCN A 203
ChainResidue
AARG82
BGLY35
BALA78
BPHE127
BHOH306

site_idAC4
Number of Residues5
Detailsbinding site for residue SCN B 201
ChainResidue
AGLY35
AALA78
APHE127
BARG82
BHOH307

site_idAC5
Number of Residues3
Detailsbinding site for residue SCN B 202
ChainResidue
APRO49
BPRO49
BHOH362

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
ChainResidueDetails
AHIS54
BHIS54

224201

PDB entries from 2024-08-28

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