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3N3D

Crystal structure of geranylgeranyl pyrophosphate synthase from lactobacillus brevis atcc 367

Functional Information from GO Data
ChainGOidnamespacecontents
A0004659molecular_functionprenyltransferase activity
A0008299biological_processisoprenoid biosynthetic process
A0016740molecular_functiontransferase activity
B0004659molecular_functionprenyltransferase activity
B0008299biological_processisoprenoid biosynthetic process
B0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 334
ChainResidue
ALYS47
AARG50
AHIS80
AARG97
ATYR211

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 335
ChainResidue
AGLN32
AHIS35
AHIS36

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 336
ChainResidue
ALYS43
ASER44
AGLY45
AGLY46
ALYS47
AARG3

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 337
ChainResidue
AHIS250
AALA251
APRO252
AARG253
AASP254

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 334
ChainResidue
BLYS47
BARG50
BHIS80
BTYR211
BHOH340

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. IGcaYQMlDDIlD
ChainResidueDetails
AILE207-ASP219

site_idPS00723
Number of Residues15
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LIhDDvi..DdsptRRG
ChainResidueDetails
ALEU84-GLY98

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PDB entries from 2024-07-24

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