MolNFT v1 · #108953 · protein

Crystal structure of the CHSH1-CHSH2 complex from mycobacterium tuberculosis bound to 3-opc-CoA

4WNB · Hydratase CHSH2: “Crystal structure of the CHSH1-CHSH2 complex from mycobacterium tuberculosis bound to 3-opc-CoA”. X-ray diffraction, 3 ligands (4BN, CD, CA), 1 pocket (best druggability 0.70). MolNFT v1 #108953 on GenesisL1: 3D…

PDB: 4WNB
Type: protein
Length: 294 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydratase CHSH2; Hydratase CHSH1
UniProt: I1SFB1, A2VPV3
Ligands: 4BN, CD, CA
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydratase CHSH2	protein	169	28% helix, 33% strand	I1SFB1
B	Hydratase CHSH1	protein	125	28% helix, 38% strand	A2VPV3

Ligands and binding sites

4BN · 3-oxo-4-pregnene-20-carboxyl-coenzyme A · ligand · chains A, B
CD · Cadmium ion · metal · 2 copies · chains A, B
CA · Calcium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	565	0.70	0.79	53	empty

Interfaces

1 interface between chains.

A–B · 1329 Å² buried · 18 hydrogen bonds · protein-protein

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 I1SFB1
Every structure of UniProt A2VPV3
Elsewhere: RCSB PDB 4WNB · PDBe 4WNB · UniProt I1SFB1 · UniProt A2VPV3

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