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3Q30

Human Squalene synthase in complex with (2R,3R)-2-Carboxymethoxy-3-[5-(2-naphthalenyl)pentyl]aminocarbonyl-3-[5-(2-naphthalenyl)pentyloxy]propionic acid

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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 600
ChainResidue
AASP80
AGLU83
AASP84
AHOH461
AHOH506
AMG601
AD61700

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AHOH599
AMG600
AD61700
AASP80
AASP84

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE D61 A 700
ChainResidue
ATYR73
AARG77
AASP80
AASP84
ATYR171
AVAL175
AALA176
AVAL179
AGLY180
ALEU183
AGLY208
AGLN212
APHE288
AHOH407
AHOH461
AHOH506
AHOH599
AMG600
AMG601

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 1
ChainResidue
AHOH19
AARG148
AARG149
AHIS173
ATYR174
AHOH376
AHOH554

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

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24531458","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
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

247536

PDB entries from 2026-01-14

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