Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4LFG

Crystal structure of geranylgeranyl diphosphate synthase sub1274 (target efi-509455) from streptococcus uberis 0140j with bound magnesium and isopentyl diphosphate, fully liganded complex;

Functional Information from GO Data
ChainGOidnamespacecontents
A0004337molecular_function(2E,6E)-farnesyl diphosphate synthase activity
A0004659molecular_functionprenyltransferase activity
A0005737cellular_componentcytoplasm
A0008299biological_processisoprenoid biosynthetic process
A0016114biological_processterpenoid biosynthetic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0004337molecular_function(2E,6E)-farnesyl diphosphate synthase activity
B0004659molecular_functionprenyltransferase activity
B0005737cellular_componentcytoplasm
B0008299biological_processisoprenoid biosynthetic process
B0016114biological_processterpenoid biosynthetic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE IPE A 301
ChainResidue
AASP78
AIPE302
AMG303
AMG304
AMG305
AHOH415
AHOH422
AHOH431
AHOH490
AHOH507
AHOH577
AASP84
AHOH578
AHOH580
AHOH639
AARG89
AGLN149
ALYS172
ATHR173
AASP213
AASP217
ALYS227

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE IPE A 302
ChainResidue
AGLY37
ALYS38
AARG41
AHIS71
ALEU75
AARG90
ATHR173
APHE209
AGLN210
AASP213
AIPE301
AHOH404
AHOH406
AHOH409
AHOH410
AHOH412
AHOH579

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 303
ChainResidue
AASP78
AASP84
AIPE301
AMG304
AHOH431
AHOH490
AHOH495

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 304
ChainResidue
AASP78
AASP84
AIPE301
AMG303
AHOH415
AHOH422

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 305
ChainResidue
AASP213
AASP217
AIPE301
AHOH507
AHOH577
AHOH578

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE IPE B 301
ChainResidue
BASP78
BASP84
BARG89
BLYS172
BTHR173
BGLN210
BASP213
BLYS227
BIPE302
BMG303
BMG304
BMG305
BHOH406
BHOH408
BHOH411
BHOH444
BHOH446
BHOH447
BHOH557
BHOH604
BHOH605

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE IPE B 302
ChainResidue
BGLY37
BLYS38
BARG41
BHIS71
BLEU75
BARG90
BTHR173
BPHE209
BGLN210
BASP213
BIPE301
BHOH404
BHOH405
BHOH409
BHOH416
BHOH419
BHOH497

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 303
ChainResidue
BHOH604
BHOH605
BASP213
BIPE301
BHOH406

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 304
ChainResidue
BASP78
BASP84
BIPE301
BMG305
BHOH444
BHOH493
BHOH557

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 305
ChainResidue
BASP78
BASP84
BIPE301
BMG304
BHOH408
BHOH411

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. IGlaFQVrDDIlD
ChainResidueDetails
AILE205-ASP217

site_idPS00723
Number of Residues17
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LIhDDlpamDnddyRRG
ChainResidueDetails
ALEU75-GLY91

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon