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3WEK

Crystal structure of the human squalene synthase F288L mutant in complex with presqualene pyrophosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004310molecular_functionfarnesyl-diphosphate farnesyltransferase activity
A0008610biological_processlipid biosynthetic process
A0009058biological_processbiosynthetic process
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0045338biological_processfarnesyl diphosphate metabolic process
A0051996molecular_functionsqualene synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP80
AGLU83
AASP84
AHOH644
AHOH647
AHOH675

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PS7 A 402
ChainResidue
APHE54
APHE72
AARG77
AASP80
AVAL175
AGLY180
ASER184
AMET207
AGLN212
AASN215
ATYR276
ACYS289
AHOH678
AHOH680
ASER51
AARG52
ASER53

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
AARG52
AARG77
AARG218
ALYS315
AARG317

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
ALEU288polar/non-polar interaction, steric role, van der waals interaction

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PDB entries from 2024-09-04

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