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Flavo di-iron protein H90A mutant from thermotoga maritima

Analyse Flavo di-iron protein H90A mutant from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DIK
Type: protein
Length: 802 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flavoprotein
UniProt: Q9WZL4
Ligands: FEO, CL
Pockets: 10 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flavoprotein	protein	402	35% helix, 26% strand	Q9WZL4
B	Flavoprotein	protein	400	34% helix, 26% strand	Q9WZL4

Ligands and binding sites

FEO · Mu-oxo-diiron · ligand · 2 copies · chains A, B
CL · Chloride ion · ion · 3 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	627	0.73	0.80	59	empty
2	206	0.64	0.83	27	empty
3	146	0.54	0.81	17	empty
4	136	0.50	0.79	18	empty
5	68	0.50	0.84	18	empty

Interfaces

1 interface between chains.

A–B · 2022 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

4DIK · Flavo Di-iron protein H90A mutant from Thermotoga maritima · 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 Q9WZL4
Elsewhere: RCSB PDB 4DIK · PDBe 4DIK · UniProt Q9WZL4

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