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

3WCA

The complex structure of TcSQS with ligand, FSPP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004310molecular_functionfarnesyl-diphosphate farnesyltransferase activity
A0004311molecular_functionfarnesyltranstransferase activity
A0008610biological_processlipid biosynthetic process
A0009058biological_processbiosynthetic process
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0004310molecular_functionfarnesyl-diphosphate farnesyltransferase activity
B0004311molecular_functionfarnesyltranstransferase activity
B0008610biological_processlipid biosynthetic process
B0009058biological_processbiosynthetic process
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
C0004310molecular_functionfarnesyl-diphosphate farnesyltransferase activity
C0004311molecular_functionfarnesyltranstransferase activity
C0008610biological_processlipid biosynthetic process
C0009058biological_processbiosynthetic process
C0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
D0004310molecular_functionfarnesyl-diphosphate farnesyltransferase activity
D0004311molecular_functionfarnesyltranstransferase activity
D0008610biological_processlipid biosynthetic process
D0009058biological_processbiosynthetic process
D0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FPS A 501
ChainResidue
ASER42
AGLN204
AASN207
AHOH786
AHOH802
AHOH831
ASER44
APHE45
ATYR64
AVAL171
AGLY172
ALEU175
AALA196
AMET199

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AASP71
AGLU74
AASP75
ATYR163

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE FPS B 401
ChainResidue
BSER42
BSER44
BPHE45
BTYR64
BARG68
BVAL171
BGLY172
BLEU175
BTYR179
BMET199
BGLY200
BLEU203
BGLN204
BASN207
BTYR270

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BASP71
BGLU74

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 403
ChainResidue
BASP71
BHOH693

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE FPS C 401
ChainResidue
CSER42
CSER44
CPHE45
CTYR64
CARG68
CGLY172
CLEU175
CALA196
CMET199
CGLY200
CLEU203
CGLN204
CASN207
CFPS402
CHOH694

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FPS C 402
ChainResidue
CPHE45
CTYR64
CARG68
CASP71
CVAL171
CGLN204
CASN207
CASP211
CASP215
CFPS401

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FPS D 401
ChainResidue
DSER42
DSER44
DPHE45
DTYR64
DVAL171
DGLY172
DLEU175
DTYR179
DMET199
DGLY200
DLEU203
DASN207

Functional Information from PROSITE/UniProt
site_idPS01044
Number of Residues16
DetailsSQUALEN_PHYTOEN_SYN_1 Squalene and phytoene synthases signature 1. YChyVAGLVGhgLtlL
ChainResidueDetails
ATYR163-LEU178

site_idPS01045
Number of Residues28
DetailsSQUALEN_PHYTOEN_SYN_2 Squalene and phytoene synthases signature 2. MGlflQkt.NIiRDFyeDicevpp.RvFwP
ChainResidueDetails
AMET199-PRO226

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon