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4KPJ

Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant complexed with Mg, Pamidronate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004659molecular_functionprenyltransferase activity
A0008299biological_processisoprenoid biosynthetic process
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE 210 A 901
ChainResidue
ALEU100
AMG902
AMG903
AMG904
AEDO906
AHOH1001
AHOH1002
AHOH1004
AHOH1005
AHOH1006
AHOH1007
AASP103
AHOH1008
AHOH1009
AHOH1015
AHOH1017
AHOH1153
AHOH1221
AASP107
AARG112
ALYS200
ATHR201
AGLN240
AASP243
ALYS257

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 902
ChainResidue
AASP103
AASP107
A210901
AMG904
AHOH1004
AHOH1005

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 903
ChainResidue
AASP243
A210901
AHOH1006
AHOH1007
AHOH1008

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 904
ChainResidue
AASP103
AASP107
A210901
AMG902
AHOH1001
AHOH1002
AHOH1003

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 905
ChainResidue
ALEU248
AILE262
ASER268
ALEU270
AVAL271
ATYR290
ATYR305
AHOH1080
AHOH1081

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 906
ChainResidue
AGLN96
ALYS200
ATHR201
AALA204
ASER205
A210901

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 907
ChainResidue
APRO151
ATYR152
ALEU154
AASN155

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 908
ChainResidue
ALEU246
AASP247
AGLY250
APRO252
ATHR255
ALYS257
AGLY259
AHOH1244

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 909
ChainResidue
AALA299
AHIS324
AHOH1195
AHOH1258

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 910
ChainResidue
AGLN282
AILE285
AARG300
AGLU307
AHOH1171

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. MGefFQIqDDYlD
ChainResidueDetails
AMET235-ASP247

site_idPS00723
Number of Residues15
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVaDDim..DssltRRG
ChainResidueDetails
ALEU100-GLY114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5
ChainResidueDetails
ALYS57
AARG60
AGLN96
AASP103
AASP107
AARG113

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AARG112
ALYS200
ATHR201
AGLN240
ALYS257

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS266

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for determining product chain length => ECO:0000250
ChainResidueDetails
APHE98
APHE99

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS57

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS287

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PDB entries from 2024-09-11

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