MolNFT v1 · #127303 · protein

Structure of the R domain of carboxylic acid reductase (car) from mycobacterium marinum in complex with NADP

5MSO: “Structure of the R domain of carboxylic acid reductase (car) from mycobacterium marinum in complex with NADP”. X-ray diffraction, 1 ligand (NAP), 2 pockets (best druggability 0.74). MolNFT v1 #127303 on GenesisL1: 3D structure…

PDB: 5MSO
Type: protein
Length: 441 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxylic acid reductase
EC: 1.2.1.-
UniProt: B2HN69
Ligands: NAP
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxylic acid reductase (EC 1.2.1.-)	protein	441	48% helix, 13% strand	B2HN69

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	891	0.74	0.78	74	NAP
2	102	0.40	0.76	26	empty

Compared structures

5MSO · Structure of the R domain of carboxylic acid reductase (CAR) from Mycobacterium marinum… · the same entry in another collection · chain A against A, TM-score 1.00
B2HN69 · AlphaFold monomer V2.0 prediction for carboxylic acid reductase (B2HN69) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 B2HN69
Elsewhere: RCSB PDB 5MSO · PDBe 5MSO · UniProt B2HN69

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