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5XJ6

Crystal structure of PlsY (YgiH), an integral membrane glycerol 3-phosphate acyltransferase - the glycerol 3-phosphate form

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006644biological_processphospholipid metabolic process
A0008654biological_processphospholipid biosynthetic process
A0016740molecular_functiontransferase activity
A0043772molecular_functionacyl-phosphate glycerol-3-phosphate acyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue G3P A 301
ChainResidue
ASER35
AHOH401
AHOH403
ATHR41
AARG45
ALYS104
AVAL138
ASER142
AHIS177
AASN180
APO4306

site_idAC2
Number of Residues9
Detailsbinding site for residue OLC A 302
ChainResidue
APHE56
ALEU110
ATRP128
APHE132
AALA145
AALA166
AVAL197
ALEU198
AGLN200

site_idAC3
Number of Residues5
Detailsbinding site for residue OLC A 303
ChainResidue
APHE83
AILE131
ATRP134
APHE152
AVAL168

site_idAC4
Number of Residues5
Detailsbinding site for residue OLC A 304
ChainResidue
ASER119
ALEU122
ATYR175
AARG178
AOLC305

site_idAC5
Number of Residues11
Detailsbinding site for residue OLC A 305
ChainResidue
ATYR11
ATYR94
APHE100
ASER117
ASER119
AVAL120
APHE152
AALA156
ATYR158
ATYR175
AOLC304

site_idAC6
Number of Residues8
Detailsbinding site for residue PO4 A 306
ChainResidue
AASN37
AGLY39
AHIS92
AGLY103
ALYS104
AGLY105
AVAL106
AG3P301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues100
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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