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Structure of CTATM1 in the occluded conformation with ATP bound

Analyse Structure of CTATM1 in the occluded conformation with ATP bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7PR1
Type: protein
Length: 1,174 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative iron-sulfur protein
UniProt: G0SBE6
Ligands: ATP, MG
Pockets: 16 · best druggability 0.89

Structure

electron microscopy · 1 distinct chain · 65% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative iron-sulfur protein	protein	587	65% helix, 10% strand	G0SBE6

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1179	0.89	0.91	110	empty
2	745	0.88	0.92	102	ATP, MG
3	142	0.77	0.95	29	empty
4	119	0.75	0.95	19	empty
5	393	0.65	0.78	37	empty

Interfaces

1 interface between chains.

A–B · 8497 Å² buried · 68 hydrogen bonds · protein-protein

Compared structures

7PR1 · Structure of CtAtm1 in the occluded conformation with ATP bound · 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 G0SBE6
Elsewhere: RCSB PDB 7PR1 · PDBe 7PR1 · UniProt G0SBE6

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