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3WEG

Crystal structure of the human squalene synthase in complex with farnesyl thiopyrophosphate and magnesium ion

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP219
AFPS405
AHOH696
AHOH697
AHOH706
AHOH707

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AFPS405
AASP80
AGLU83
AASP84

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AASP80
AASP84
AFPS405

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FPS A 404
ChainResidue
ATHR50
ASER51
ASER53
APHE54
ATYR73
AARG77
AGLY180
AMET207
AGLN212
AASN215
ATYR276
AFPS405

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FPS A 405
ChainResidue
APHE54
ATYR73
ALEU76
AARG77
AASP80
AASP84
AVAL175
ALEU183
AGLN212
AMG401
AMG402
AMG403
AFPS404
AHOH706

Functional Information from PROSITE/UniProt
site_idPS01044
Number of Residues16
DetailsSQUALEN_PHYTOEN_SYN_1 Squalene and phytoene synthases signature 1. YChyVAGLVGigLsrL
ChainResidueDetails
ATYR171-LEU186

site_idPS01045
Number of Residues26
DetailsSQUALEN_PHYTOEN_SYN_2 Squalene and phytoene synthases signature 2. MGlflQkt.NIiRDYleDqqgg...ReFwP
ChainResidueDetails
AMET207-PRO232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ASER284-TYR304

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:24531458
ChainResidueDetails
ALYS315
AARG317
AARG52
AARG77
AARG218

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:24531458, ECO:0007744|PDB:3WEG, ECO:0007744|PDB:3WEH
ChainResidueDetails
AASP80
AGLU83
AASP84

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 264
ChainResidueDetails
ATYR171hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG218electrostatic stabiliser, hydrogen bond donor, promote heterolysis
AARG228electrostatic stabiliser, hydrogen bond donor, promote heterolysis
APHE288polar/non-polar interaction, steric role, van der waals interaction

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PDB entries from 2024-05-29

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