Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5F2Z

Crystal structure of membrane associated PatA from Mycobacterium smegmatis in complex with palmitate - P21 space group

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0008654biological_processphospholipid biosynthetic process
A0009247biological_processglycolipid biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0046488biological_processphosphatidylinositol metabolic process
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0008654biological_processphospholipid biosynthetic process
B0009247biological_processglycolipid biosynthetic process
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0046488biological_processphosphatidylinositol metabolic process
C0005886cellular_componentplasma membrane
C0006629biological_processlipid metabolic process
C0008654biological_processphospholipid biosynthetic process
C0009247biological_processglycolipid biosynthetic process
C0016020cellular_componentmembrane
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0046488biological_processphosphatidylinositol metabolic process
D0005886cellular_componentplasma membrane
D0006629biological_processlipid metabolic process
D0008654biological_processphospholipid biosynthetic process
D0009247biological_processglycolipid biosynthetic process
D0016020cellular_componentmembrane
D0016740molecular_functiontransferase activity
D0016746molecular_functionacyltransferase activity
D0046488biological_processphosphatidylinositol metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue PLM A 401
ChainResidue
AHIS126
ATRP130
AALA133
AGLY134
AARG164
ACYS196
AMET198
AVAL250

site_idAC2
Number of Residues10
Detailsbinding site for residue PLM B 401
ChainResidue
BHIS126
BTRP130
BGLY134
BPHE144
BTHR146
BARG164
BCYS196
BMET198
BHOH519
BVAL104

site_idAC3
Number of Residues9
Detailsbinding site for residue PLM C 401
ChainResidue
CLEU124
CHIS126
CTRP130
CALA133
CGLY134
CARG164
CCYS196
CMET198
CVAL250

site_idAC4
Number of Residues6
Detailsbinding site for residue PLM D 401
ChainResidue
DHIS126
DTRP130
DALA133
DGLY134
DARG164
DCYS196

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694
ChainResidueDetails
AHIS126
BHIS126
CHIS126
DHIS126

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694
ChainResidueDetails
AGLU200
BGLU200
CGLU200
DGLU200

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000305|PubMed:26965057
ChainResidueDetails
AHIS126
CARG164
CSER206
CGLU229
DHIS126
DARG164
DSER206
DGLU229
AARG164
ASER206
AGLU229
BHIS126
BARG164
BSER206
BGLU229
CHIS126

218853

건을2024-04-24부터공개중

PDB statisticsPDBj update infoContact PDBjnumon