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3VJA

Crystal structure of the human squalene synthase

Functional Information from GO Data
ChainGOidnamespacecontents
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 [NAD(P)H] activity
B0008610biological_processlipid biosynthetic process
B0009058biological_processbiosynthetic process
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0045338biological_processfarnesyl diphosphate metabolic process
B0051996molecular_functionsqualene synthase [NAD(P)H] activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A 401
ChainResidue
AHIS98
AGLU343
AHIS347
AHOH455
AHOH466

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI B 401
ChainResidue
BHIS98
BGLU343
BHIS347
BHOH451

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 Residues40
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24531458","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24531458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3WEG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WEH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

site_idMCSA2
Number of Residues4
DetailsM-CSA 264
ChainResidueDetails
BTYR171hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BARG218electrostatic stabiliser, hydrogen bond donor, promote heterolysis
BARG228electrostatic stabiliser, hydrogen bond donor, promote heterolysis
BPHE288polar/non-polar interaction, steric role, van der waals interaction

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PDB entries from 2025-12-24

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