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The crystal structure of encm

Analyse The crystal structure of encm in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3W8W
Type: protein
Length: 921 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative FAD-dependent oxygenase encm
EC: 1.13.12.-
UniProt: Q9KHK2
Ligands: FAD
Pockets: 6 · best druggability 0.89

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative FAD-dependent oxygenase encm (EC 1.13.12.-)	protein	460	35% helix, 24% strand	Q9KHK2
B	Putative FAD-dependent oxygenase encm (EC 1.13.12.-)	protein	461	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

6 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	840	0.89	0.91	108	FAD
2	924	0.88	0.90	108	FAD
3	403	0.77	0.86	51	empty
4	392	0.77	0.87	43	empty
5	311	0.61	0.79	43	empty

Interfaces

1 interface between chains.

A–B · 2279 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

3W8W · The crystal structure of EncM · 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 3W8W · PDBe 3W8W · UniProt Q9KHK2

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