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Crystal structure of MHPCO, Y270F mutant

Analyse Crystal structure of MHPCO, Y270F mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4H2N
Type: protein
Length: 370 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.302
Source: Rhizobium loti
Molecule: 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
EC: 1.14.12.4
UniProt: Q988D3
Ligands: FAD
Pockets: 2 · best druggability 0.81

Structure

x-ray diffraction · resolution 2.302 · 1 distinct chain · 35% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (EC 1.14.12.4)	protein	370	35% helix, 28% strand	Q988D3

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
BME · Beta-mercaptoethanol · additive · chains A
GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	951	0.81	0.82	83	FAD, BME
2	92	0.36	0.75	18	empty

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

4H2N · Crystal structure of mhpco, Y270F mutant · 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 Q988D3
Elsewhere: RCSB PDB 4H2N · PDBe 4H2N · UniProt Q988D3

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