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3W7F

Crystal structure of the C(30) carotenoid dehydrosqualene synthase from staphylococcus aureus complexed with farnesyl thiopyrophosphate

Replaces:  2ZCP
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
B0003824molecular_functioncatalytic activity
B0004311molecular_functionfarnesyltranstransferase activity
B0009058biological_processbiosynthetic process
B0016117biological_processcarotenoid biosynthetic process
B0016120biological_processcarotene biosynthetic process
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0016767molecular_functiongeranylgeranyl-diphosphate geranylgeranyltransferase activity
B0046872molecular_functionmetal ion binding
B0046905molecular_function15-cis-phytoene synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FPS A 301
ChainResidue
ATYR41
AFPS302
AMG303
AMG304
AMG305
AHOH401
AHOH402
AHOH403
AHOH405
AHOH406
AHOH407
ACYS44
AARG45
AASP48
AVAL137
ALEU141
AASN168
AARG171
AASP172

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE FPS A 302
ChainResidue
AHIS18
ASER19
ALYS20
ASER21
APHE22
ATYR41
AARG45
AALA157
AGLN165
AARG171
ATYR248
AARG265
AFPS301
AMG304
AHOH407

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 303
ChainResidue
AASN168
AASP172
AFPS301
AHOH402
AHOH403
AHOH408

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 304
ChainResidue
AFPS301
AFPS302
AHOH406
AHOH407

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 305
ChainResidue
AASP48
AASP52
AFPS301
AHOH401
AHOH404
AHOH405

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FPS B 301
ChainResidue
BPHE26
BTYR41
BCYS44
BARG45
BASP48
BASN168
BARG171
BASP172
BFPS302
BMG303
BMG304
BMG305
BHOH401
BHOH402
BHOH403
BHOH404
BHOH405
BHOH408
BHOH409

site_idAC7
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FPS B 302
ChainResidue
BSER19
BLYS20
BSER21
BPHE22
BTYR41
BARG45
BLEU145
BALA157
BLEU160
BGLY161
BARG171
BPHE233
BTYR248
BARG265
BFPS301
BMG304
BHOH403
BHOH408

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 303
ChainResidue
BASN168
BASP172
BFPS301
BHOH404
BHOH406
BHOH409

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 304
ChainResidue
BFPS301
BFPS302
BHOH403
BHOH408

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 305
ChainResidue
BFPS301
BHOH401
BHOH407
BHOH574
BASP48
BASP52

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 Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCS, ECO:0007744|PDB:3W7F
ChainResidueDetails
AHIS18
ATYR41
BHIS18
BTYR41

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F
ChainResidueDetails
AARG45
BARG45

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F
ChainResidueDetails
AASP48
AASP52
BASP48
BASP52

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:2ZCR
ChainResidueDetails
AGLN165
BGLN165

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:2ZCR, ECO:0007744|PDB:3W7F
ChainResidueDetails
AASN168
AASP172
BASN168
BASP172

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:3W7F
ChainResidueDetails
AARG171
ATYR248
BARG171
BTYR248

222036

PDB entries from 2024-07-03

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