Structure of PDB 4gp2 Chain B

Receptor sequence
>4gp2B (length=331) Species: 410359 (Pyrobaculum calidifontis JCM 11548) [Search protein sequence]
DVVSRLHQKYGAEVEKALVRYLSIGLAEDFREAVLYQVKTGGKRLRPLLT
LAAAEAVSGQWRPALPAAAIVELIHNYSLIYDDIIDRGDVRRGLPTVRKA
FGDNAAILVGIWYREAIEEAVLDTPKPTLFAKEVAEVIKAIDEGERLDIL
FEAAGRSDPYFVQARWREVTLDDYIKMVSLKTGALIAAAAKWGVLSVSDD
RGLAEAAWNFGMAAGVAFQIIDDVLDIYGDEIGKDIKEHKRGNAVVAVAL
SHLGEGERRRLLEILAREVVEEADVREAVALLDSVGAREEALRLAARYRE
EAERHLAKIPNNGTLKELLDFIVAREYAENL
3D structure
PDB4gp2 Crystal Structure of Isoprenoid Synthase from Pyrobaculum Calidifontis
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K46 Y80 D85 D89 R94 L150 K179 F221 D225 D226
Catalytic site (residue number reindexed from 1) K43 Y77 D82 D86 R91 L147 K176 F218 D222 D223
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG B D85 D89 D82 D86
BS02 MG B D85 D89 D82 D86
BS03 MG B D225 D229 D222 D226
BS04 DMA B S81 D85 R94 K184 S78 D82 R91 K181
BS05 DMA B K46 R49 H78 R95 F221 K43 R46 H75 R92 F218
Gene Ontology
Molecular Function
GO:0004311 farnesyltranstransferase activity
GO:0004659 prenyltransferase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0008299 isoprenoid biosynthetic process
GO:0033386 geranylgeranyl diphosphate biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4gp2, PDBe:4gp2, PDBj:4gp2
PDBsum4gp2
PubMed
UniProtA3MSH1

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