Structure of PDB 8a7j Chain A

Receptor sequence
>8a7jA (length=345) Species: 80249 (Phaedon cochleariae) [Search protein sequence]
SFSKEESREFMAIFPDIVRDLTDAGRHTDIPEVTKRFAKVLQYNVPTGKK
TRGLSTVIAYKMLEKPENLTPENVRLAGILGWCVELLQASLLIMDDLMDR
SETRRGQPCWYRQENVGFLAINDCLHVESSLYSVLRKYFSHLPCYVPIIE
LFHDVNFKTNMGQSLDALCMKDGRPILSQFTMKRYSSIVKYKTSYYTFQL
PVSLGMYLADMYDPEQHRQAKTILMEIGEFFQIQDDFLDAFGDSQVTGKV
GTDIKEGKCSWLAVVALQRSNPAQRQIMEEHYGRPEPESTQIIKNLYIEL
GLPATFAVYEEESFNIIRTHIHQISKGLPHDLFFKIMKKIYKRDA
3D structure
PDB8a7j Metal-dependent enzyme symmetry guides the biosynthetic flux of terpene precursors.
ChainA
Resolution1.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.1: dimethylallyltranstransferase.
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 MN A D179 D183 D95 D99
BS02 MN A D179 D183 D95 D99
BS03 IPE A K133 R136 Q172 R189 T277 F315 D319 K49 R52 Q88 R105 T193 F231 D235
BS04 ZOL A D179 R188 Q247 K276 T277 D319 K333 D95 R104 Q163 K192 T193 D235 K249
Gene Ontology
Molecular Function
GO:0004659 prenyltransferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
Biological Process
GO:0008299 isoprenoid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:8a7j, PDBe:8a7j, PDBj:8a7j
PDBsum8a7j
PubMed37308711
UniProtM1JS91

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