Structure of PDB 7c8z Chain E

Receptor sequence
>7c8zE (length=383) Species: 54061 (Ralstonia sp.) [Search protein sequence]
PVFPQDPKWPGEGSSRVPFWAYTREDLYKRELERLFYANHWCYVGLEAEI
PNPGDFKRTVIGERSVIMVRDPDGGINVVENVCAHRGMRFCRERHGNAKD
FFCPYHQWNYSLKGDLQGVPFRRGVKQDGKVNGGMPKDFKLEEHGLTKLK
VAARGGAVFASFDHDVEPFEEFLGPTILHYFDRVFNGRKLKILGYRRQRI
PGNWKLMQENIKDPYHPGLLHTWFKSELKMDAKFRHAAMISTVNDPRLLD
IVPEPWWGGPTAVMTTIFPSVIIQQQVNSVSTRHIQPNGHGSFDFVWTHF
GFEDDNEEWTQRRLIQANLFGPAGFVSADDGEVIEWSQEGFEQKPTHRTV
IEMGGHEIGDTDHMVTETLIRGMYDYWRKVMGE
3D structure
PDB7c8z Structural and Biochemical Analysis Reveals a Distinct Catalytic Site of Salicylate 5-Monooxygenase NagGH from Rieske Dioxygenases.
ChainE
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H114 D221 H224 H229 D370
Catalytic site (residue number reindexed from 1) H106 D213 H216 H221 D330
Enzyme Commision number 1.14.13.172: salicylate 5-hydroxylase.
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 FES E C91 H93 R94 C111 Y113 H114 W116 C83 H85 R86 C103 Y105 H106 W108
BS02 FE E H224 H229 D370 H216 H221 D330
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0034785 salicylate 5-hydroxylase activity
GO:0046872 metal ion binding
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0009056 catabolic process
GO:0044237 cellular metabolic process
GO:0046244 salicylic acid catabolic process
Cellular Component
GO:1902494 catalytic complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7c8z, PDBe:7c8z, PDBj:7c8z
PDBsum7c8z
PubMed33452034
UniProtO52379|NAGG_RALSP Salicylate 5-hydroxylase, large oxygenase component (Gene Name=nagG)

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