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Crystal structure of methanothermobacter thermautotrophicus cbil

Analyse Crystal structure of methanothermobacter thermautotrophicus cbil in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QBU
Type: protein
Length: 456 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Precorrin-2 methyltransferase
UniProt: O27402
Ligands: SAH
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Precorrin-2 methyltransferase	protein	228	36% helix, 22% strand	O27402

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	706	0.77	0.82	50	SAH
2	590	0.75	0.81	48	SAH
3	56	0.39	0.81	15	empty

Interfaces

1 interface between chains.

A–B · 2276 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

2QBU · Crystal structure of Methanothermobacter thermautotrophicus CbiL · the same entry in another collection · chain B against B, 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 O27402
Elsewhere: RCSB PDB 2QBU · PDBe 2QBU · UniProt O27402

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