MolNFT v1 · #153098 · protein

Crystal structure of CMIS2

6J38 · FAD-dependent glycine oxydase: “Crystal structure of CMIS2”. X-ray diffraction, 1 ligand (FAD), 4 pockets (best druggability 0.84). MolNFT v1 #153098 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6J38
Type: protein
Length: 724 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FAD-dependent glycine oxydase
UniProt: X5IYZ1
Ligands: FAD
Pockets: 4 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FAD-dependent glycine oxydase	protein	368	36% helix, 27% strand	X5IYZ1
B	FAD-dependent glycine oxydase	protein	356	37% helix, 27% strand	X5IYZ1

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

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	739	0.84	0.87	97	FAD
2	571	0.79	0.85	77	FAD
3	652	0.75	0.81	46	empty
4	113	0.44	0.78	22	empty

Interfaces

1 interface between chains.

A–B · 388 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6J38 · Crystal structure of CmiS2 · 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 X5IYZ1
Elsewhere: RCSB PDB 6J38 · PDBe 6J38 · UniProt X5IYZ1

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