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4N9U

The role of lysine 200 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates

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 Residues7
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP103
AASP107
AMG403
ARIS404
AHOH553
AHOH554
AHOH581

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AHOH550
AHOH551
AHOH552
AHOH582
AASP243
ARIS404

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AASP103
AASP107
AMG401
ARIS404
AHOH556
AHOH557
AHOH558

site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE RIS A 404
ChainResidue
ALEU100
AASP103
AASP107
AARG112
AGLN171
AGLY200
ATHR201
AGLN240
AASP243
ALYS257
AMG401
AMG402
AMG403
AHOH540
AHOH549
AHOH550
AHOH551
AHOH552
AHOH554
AHOH557
AHOH558
AHOH562
AHOH563
AHOH579
AHOH581
AHOH582

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 405
ChainResidue
AGLU136
AALA137
ATYR140
ALEU161
ASER164
AHOH523
AHOH564

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 406
ChainResidue
AARG141
AGLN162
AHOH523
AHOH608

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
AGLY200
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 2024-10-30

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