Structure of PDB 2std Chain A

Receptor sequence
>2stdA (length=162) Species: 148305 (Pyricularia grisea) [Search protein sequence]
DEITFSDYLGLMTCVYEWADSYDSKDWDRLRKVIAPTLRIDYRSFLDKLW
EAMPAEEFVGMVSSKQVLGDPTLRTQHFIGGTRWEKVSEDEVIGYHQLRV
PHQRYKDTTMKEVTMKGHAHSANLHWYKKIDGVWKFAGLKPDIRWGEFDF
DRIFEDGRETFG
3D structure
PDB2std Cryogenic X-ray crystal structure analysis for the complex of scytalone dehydratase of a rice blast fungus and its tight-binding inhibitor, carpropamid: the structural basis of tight-binding inhibition.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y30 D31 Y50 H85 H110
Catalytic site (residue number reindexed from 1) Y22 D23 Y42 H77 H102
Enzyme Commision number 4.2.1.94: scytalone dehydratase.
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 CRP A W26 Y50 V75 L76 F158 W18 Y42 V67 L68 F150 MOAD: Kd=0.14nM
PDBbind-CN: -logKd/Ki=9.85,Ki=0.14nM
BindingDB: Ki=30nM
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0030411 scytalone dehydratase activity
GO:0046872 metal ion binding
Biological Process
GO:0006582 melanin metabolic process
GO:0042438 melanin biosynthetic process
Cellular Component
GO:0005575 cellular_component
GO:0005768 endosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2std, PDBe:2std, PDBj:2std
PDBsum2std
PubMed9665698
UniProtP56221|SCYD_PYRO7 Scytalone dehydratase (Gene Name=SDH1)

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