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4F6V

Crystal structure of dehydrosqualene synthase (crtm) from s. aureus complexed with bph-1034, mg2+ and fmp.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004311molecular_functionfarnesyltranstransferase activity
A0009058biological_processbiosynthetic process
A0016117biological_processcarotenoid biosynthetic process
A0016120biological_processcarotene biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0016767molecular_functiongeranylgeranyl-diphosphate geranylgeranyltransferase activity
A0046872molecular_functionmetal ion binding
A0046905molecular_function15-cis-phytoene synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ZYM A 301
ChainResidue
APHE22
AARG171
AASP172
AFJP303
AMG304
AMG305
AHOH496
ATYR41
ACYS44
AARG45
AASP48
AVAL133
AVAL137
AGLN165
AASN168

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SRT A 302
ChainResidue
AHIS18
ASER19
ALYS20
ASER21
AARG171
AARG265
AFJP303
AMG304
AHOH410
AHOH490

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE FJP A 303
ChainResidue
ASER19
APHE22
APHE26
ATYR41
AARG45
AALA134
AGLY138
ALEU160
AGLY161
ALEU164
AASN168
ATYR248
AZYM301
ASRT302
AMG304

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 304
ChainResidue
AASN168
AARG171
ATYR248
AZYM301
ASRT302
AFJP303

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 305
ChainResidue
AASN168
AASP172
AZYM301
AHOH495
AHOH496

Functional Information from PROSITE/UniProt
site_idPS01044
Number of Residues16
DetailsSQUALEN_PHYTOEN_SYN_1 Squalene and phytoene synthases signature 1. YCygVAGTVGevLtpI
ChainResidueDetails
ATYR129-ILE144

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCS, ECO:0007744|PDB:3W7F
ChainResidueDetails
AHIS18
ATYR41

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F
ChainResidueDetails
AARG45

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F
ChainResidueDetails
AASP48
AASP52

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:2ZCR
ChainResidueDetails
AGLN165

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:2ZCR, ECO:0007744|PDB:3W7F
ChainResidueDetails
AASN168
AASP172

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:3W7F
ChainResidueDetails
AARG171
ATYR248

220113

PDB entries from 2024-05-22

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