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Crystal structure of aclr, a thioredoxin oxidoreductase fold protein carrying the cxxh catalytic motif

Analyse Crystal structure of aclr, a thioredoxin oxidoreductase fold protein carrying… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BR0
Type: protein
Length: 318 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PYR_REDOX_2 domain-containing protein
UniProt: B8NI43
Ligands: FAD
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PYR_REDOX_2 domain-containing protein	protein	318	29% helix, 27% strand	B8NI43

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	407	0.80	0.89	54	FAD
2	174	0.45	0.75	22	empty
3	57	0.35	0.78	15	empty

Compared structures

7BR0 · Crystal structure of AclR, a thioredoxin oxidoreductase fold protein carrying the CXXH… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt B8NI43
Elsewhere: RCSB PDB 7BR0 · PDBe 7BR0 · UniProt B8NI43

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