MolNFT v1 · #126472 · protein

Structure of thermus thermophilus L-proline dehydrogenase lacking alpha helices a, B and C

5M42: “Structure of thermus thermophilus L-proline dehydrogenase lacking alpha helices a, B and C”. X-ray diffraction, 1 ligand (FMN), 1 pocket (best druggability 0.55). MolNFT v1 #126472 on GenesisL1: 3D structure, binding sites and…

PDB: 5M42
Type: protein
Length: 242 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proline dehydrogenase
EC: 1.5.5.2
UniProt: Q72IB8
Ligands: FMN
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proline dehydrogenase (EC 1.5.5.2)	protein	242	51% helix, 20% strand	Q72IB8

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 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	208	0.55	0.78	22	FMN

Compared structures

5M42 · Structure of Thermus thermophilus L-proline dehydrogenase lacking alpha helices A, B and C · the same entry in another collection · chain A against A, TM-score 1.00
Q72IB8 · AlphaFold monomer V2.0 prediction for proline dehydrogenase (Q72IB8) · a predicted model of the same protein · 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 Q72IB8
Elsewhere: RCSB PDB 5M42 · PDBe 5M42 · UniProt Q72IB8

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