Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4JZB

Crystal Structure of Leshmaniasis major Farnesyl diphosphate synthase in complex with 1-(2-HYDROXY-2,2-DIPHOSPHONOETHYL)-3-PHENYLPYRIDINIUM, IPP and Ca2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004161molecular_functiondimethylallyltranstransferase activity
A0004337molecular_functiongeranyltranstransferase activity
A0005737cellular_componentcytoplasm
A0008299biological_processisoprenoid biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0045337biological_processfarnesyl diphosphate biosynthetic process
A0046872molecular_functionmetal ion binding
B0004161molecular_functiondimethylallyltranstransferase activity
B0004337molecular_functiongeranyltranstransferase activity
B0005737cellular_componentcytoplasm
B0008299biological_processisoprenoid biosynthetic process
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0045337biological_processfarnesyl diphosphate biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP98
AASP102
ACA402
AP2H405
AHOH502
AHOH503

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AP2H405
AHOH501
AHOH504
AHOH511
AASP98
AASP102
ACA401

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP250
AP2H405
AHOH505
AHOH506
AHOH512

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE IPE A 404
ChainResidue
AGLY47
ALYS48
AARG51
AGLN91
AARG108
ATHR208
ATYR211
APHE246
AGLN247
AASP250
AP2H405
AHOH509
AHOH531
AHOH536
AHOH552
AHOH587
AHOH617
AHOH645

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE P2H A 405
ChainResidue
APHE94
AASP98
AMET101
AASP102
AARG107
ATHR163
AGLN167
ALYS207
ATHR208
AASP250
ALYS264
ACA401
ACA402
ACA403
AIPE404
AHOH504
AHOH513
AHOH532

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 406
ChainResidue
AGLY266
AGLU270
AHOH554
AHOH561
AHOH671

site_idAC7
Number of Residues18
DetailsBINDING SITE FOR RESIDUE IPE B 401
ChainResidue
BGLY47
BLYS48
BARG51
BGLN91
BARG108
BTHR208
BTYR211
BPHE246
BGLN247
BASP250
BP2H402
BHOH509
BHOH523
BHOH527
BHOH542
BHOH580
BHOH622
BHOH651

site_idAC8
Number of Residues18
DetailsBINDING SITE FOR RESIDUE P2H B 402
ChainResidue
BPHE94
BASP98
BMET101
BASP102
BARG107
BTHR163
BGLN167
BLYS207
BTHR208
BASP250
BLYS264
BIPE401
BCA403
BCA404
BCA405
BHOH504
BHOH513
BHOH545

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
BHOH503
BHOH511
BASP98
BASP102
BP2H402
BCA405

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BASP250
BP2H402
BHOH505
BHOH506
BHOH514

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 405
ChainResidue
BASP98
BASP102
BP2H402
BCA403
BHOH502
BHOH504
BHOH512

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 406
ChainResidue
BGLY266
BGLU270
BHOH562
BHOH615
BHOH766

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. MGeyFQVqDDVmD
ChainResidueDetails
AMET242-ASP254

site_idPS00723
Number of Residues15
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVeDDim..DhsktRRG
ChainResidueDetails
ALEU95-GLY109

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon