MolNFT v1 · #83851 · protein

Hcge from methanothermobacter marburgensis

3WV7 · Hmd co-occurring protein hcge: “Hcge from methanothermobacter marburgensis”. X-ray diffraction, 1 ligand (ADP), 4 pockets (best druggability 0.82). MolNFT v1 #83851 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3WV7
Type: protein
Length: 603 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hmd co-occurring protein hcge
EC: 2.7.7.-
UniProt: D9PY12
Ligands: ADP
Pockets: 4 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Hmd co-occurring protein hcge (EC 2.7.7.-)	protein	201	37% helix, 18% strand	D9PY12

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A, C

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1055	0.82	0.83	53	empty
2	380	0.72	0.83	46	empty
3	399	0.70	0.81	43	ADP
4	279	0.64	0.81	32	empty

Interfaces

3 interfaces between chains.

A–C · 1033 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 1032 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 1010 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

3WV7 · HcgE from Methanothermobacter marburgensis · 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 D9PY12
Elsewhere: RCSB PDB 3WV7 · PDBe 3WV7 · UniProt D9PY12

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