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Thermotoga maritima reverse gyrase, C2 form 2

Analyse Thermotoga maritima reverse gyrase, C2 form 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DDT
Type: protein
Length: 1,102 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Reverse gyrase
EC: 3.6.4.12, 5.99.1.3
UniProt: O51934
Ligands: ZN
Pockets: 15 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Reverse gyrase (EC 3.6.4.12, 5.99.1.3)	protein	1102	41% helix, 19% strand	O51934

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	828	0.75	0.79	72	empty
2	859	0.73	0.78	70	empty
3	203	0.62	0.82	30	empty
4	463	0.60	0.75	49	empty
5	240	0.55	0.78	29	empty

Compared structures

4DDT · Thermotoga maritima reverse gyrase, C2 FORM 2 · the same entry in another collection · chain A against A, TM-score 1.00
O51934 · AlphaFold monomer V2.0 prediction for reverse gyrase (O51934) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 O51934
Elsewhere: RCSB PDB 4DDT · PDBe 4DDT · UniProt O51934

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