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ATP-bound hcge from methanothermobacter marburgensis

Analyse ATP-bound hcge from methanothermobacter marburgensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WV8
Type: protein
Length: 402 residues
Chains: 2
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: ATP, SO4
Pockets: 3 · best druggability 0.66

Structure

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

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

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	450	0.66	0.78	61	empty
2	323	0.64	0.80	39	ATP
3	306	0.63	0.79	40	ATP

Interfaces

1 interface between chains.

A–B · 775 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

3WV8 · ATP-bound 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 3WV8 · PDBe 3WV8 · UniProt D9PY12

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