MolNFT v1 · #189744 · protein

Anaerobic hydroxyproline degradation involving C-N cleavage by a glycyl radical enzyme

7VUA · Hplg: “Anaerobic hydroxyproline degradation involving C-N cleavage by a glycyl radical enzyme”. X-ray diffraction, 1 ligand (UY7), 14 pockets (best druggability 0.76). MolNFT v1 #189744 on GenesisL1: 3D structure, binding sites and…

PDB: 7VUA
Type: protein
Length: 1,570 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hplg
UniProt: A0A316Q2B4
Ligands: UY7
Pockets: 14 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hplg	protein	785	49% helix, 9% strand	A0A316Q2B4

Ligands and binding sites

UY7 · (4S)-4-hydroxy-D-proline · ligand · 2 copies · chains A, B

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

Pockets

14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	126	0.76	0.95	27	empty
2	87	0.76	0.98	25	empty
3	333	0.74	0.86	60	empty
4	63	0.72	0.98	24	empty
5	369	0.63	0.79	32	empty

Interfaces

1 interface between chains.

A–B · 1976 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

7VUA · Anaerobic hydroxyproline degradation involving C-N cleavage by a glycyl radical enzyme · 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 A0A316Q2B4
Elsewhere: RCSB PDB 7VUA · PDBe 7VUA · UniProt A0A316Q2B4

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