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Crystal structure of tmm from myroides profundi D25

Analyse Crystal structure of tmm from myroides profundi D25 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KBW
Type: protein
Length: 892 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Trimethylamine monooxygenase
UniProt: A0A0B5RNJ4
Ligands: NAP, FAD
Pockets: 11 · best druggability 0.91

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Trimethylamine monooxygenase	protein	446	32% helix, 21% strand	A0A0B5RNJ4

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
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

11 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	1103	0.91	0.94	141	FAD
2	261	0.79	0.91	43	empty
3	209	0.62	0.82	20	empty
4	155	0.59	0.83	20	empty
5	132	0.50	0.80	17	empty

Interfaces

1 interface between chains.

A–B · 1816 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

6KBW · Crystal structure of Tmm from Myroides profundi D25 · 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 A0A0B5RNJ4
Elsewhere: RCSB PDB 6KBW · PDBe 6KBW · UniProt A0A0B5RNJ4

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