Structure of PDB 5c3q Chain A

Receptor sequence
>5c3qA (length=335) Species: 5141 (Neurospora crassa) [Search protein sequence]
GSMEKAAVNEDGLVIPLIDFSKFLEGDETLKLETAKAILHGFQTAGFIYL
KNIPIQPDFREHVFNTSAKFFKLPKEKKLEVGWTTPEANRGYSAPGREKV
TQLTDPAEIEKIRSAAPDIKESYEIGREDEPGHPNPWPAEQDDLVGFKST
MNNFFDQCKALHIEVMRAIAVGMGIDANYFDSFVDVGDNILRLLHYPAVK
SEVFKINPGQVRAGEHTDYGSITLLFQDSRGGLQVKSPNGQFIDATPIEN
TVVVNAGDLLARWSNDTIKSTVHRVVEPPKQEDVHPPRYSIAYFCNPNHK
SYIEAIPGTYAAESERKYEGINSGKYLVQRLAATY
3D structure
PDB5c3q Molecular basis for the substrate specificity and catalytic mechanism of thymine-7-hydroxylase in fungi
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R190 A211 H214 D216 H271
Catalytic site (residue number reindexed from 1) R192 A213 H216 D218 H273
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 AKG A R190 L192 Y194 H214 L223 H271 V273 R286 S288 F292 R192 L194 Y196 H216 L225 H273 V275 R288 S290 F294 MOAD: Kd=34.4uM
BS02 TDR A R190 D216 Y217 F292 R192 D218 Y219 F294 MOAD: Kd=32uM
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0044283 small molecule biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5c3q, PDBe:5c3q, PDBj:5c3q
PDBsum5c3q
PubMed26429971
UniProtQ7RYZ9

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