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4KQ5

Crystal Structure of Human Farnesyl Pyrophosphate Synthase Mutant (Y204A) Complexed with Mg and Zoledronate

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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP103
AASP107
AMG403
AZOL404
AHOH584
AHOH585

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AHOH587
AHOH588
AASP243
AZOL404
AHOH586

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AASP103
AASP107
AMG401
AZOL404
AHOH589
AHOH590
AHOH591

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ZOL A 404
ChainResidue
ALEU100
AASP103
AASP107
AARG112
AGLN171
ALYS200
ATHR201
AGLN240
AASP243
ALYS257
AMG401
AMG402
AMG403
AHOH506
AHOH584
AHOH585
AHOH586
AHOH587
AHOH588
AHOH590
AHOH591
AHOH606
AHOH607
AHOH622

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 405
ChainResidue
ATYR119
AGLY125
ALEU126
AHOH553

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 2024-11-13

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