Research workbench

Cobr in complex with FAD

Analyse Cobr in complex with FAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IRA
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-hydroxyphenylacetate 3-monooxygenase
EC: 1.14.13.3
UniProt: Q8YHT7
Ligands: FAD, SO4
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-hydroxyphenylacetate 3-monooxygenase (EC 1.14.13.3)	protein	162	18% helix, 46% strand	Q8YHT7

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A
SO4 · Sulfate ion · ion · 7 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	260	0.50	0.74	32	FAD
2	67	0.35	0.76	16	empty

Compared structures

4IRA · CobR in complex with FAD · 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 Q8YHT7
Elsewhere: RCSB PDB 4IRA · PDBe 4IRA · UniProt Q8YHT7

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