MolNFT v1 · #149362 · protein

The crystal structure of encm under anaerobic conditions

6FYA · Putative FAD-dependent oxygenase encm: “The crystal structure of encm under anaerobic conditions”. X-ray diffraction, 1 ligand (FAD), 5 pockets (best druggability 0.89). MolNFT v1 #149362 on GenesisL1: 3D structure, binding sites…

PDB: 6FYA
Type: protein
Length: 916 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative FAD-dependent oxygenase encm
UniProt: Q9KHK2
Ligands: FAD
Pockets: 5 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative FAD-dependent oxygenase encm	protein	458	35% helix, 24% strand	Q9KHK2

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	690	0.89	0.93	93	FAD
2	722	0.88	0.92	90	FAD
3	358	0.79	0.89	42	empty
4	392	0.79	0.88	52	empty
5	352	0.64	0.79	42	empty

Interfaces

1 interface between chains.

A–B · 2200 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

6FYA · The crystal structure of EncM under anaerobic conditions · 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 Q9KHK2
Elsewhere: RCSB PDB 6FYA · PDBe 6FYA · UniProt Q9KHK2

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