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Crystal structure of putative chlorite dismutase TA0507

Analyse Crystal structure of putative chlorite dismutase TA0507 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DTZ
Type: protein
Length: 1,097 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative chlorite dismutase TA0507
UniProt: Q9HKT8
Pockets: 19 · best druggability 0.73

Structure

x-ray diffraction · 4 distinct chains · 40% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative chlorite dismutase TA0507	protein	215	40% helix, 31% strand	Q9HKT8
B	Putative chlorite dismutase TA0507	protein	221	39% helix, 28% strand	Q9HKT8
C	Putative chlorite dismutase TA0507	protein	215	39% helix, 30% strand	Q9HKT8
D, E	Putative chlorite dismutase TA0507	protein	223	42% helix, 30% strand	Q9HKT8

Ligands and binding sites

FMT · Formic acid · additive · 3 copies · chains A, B, C

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

Pockets

19 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	647	0.73	0.80	50	empty
2	616	0.73	0.80	44	empty
3	513	0.71	0.80	60	empty
4	472	0.70	0.80	48	empty
5	512	0.69	0.79	44	empty

Interfaces

5 interfaces between chains.

A–B · 1646 Å² buried · 29 hydrogen bonds · protein-protein
B–C · 1641 Å² buried · 25 hydrogen bonds · protein-protein
A–E · 1636 Å² buried · 30 hydrogen bonds · protein-protein
D–E · 1604 Å² buried · 25 hydrogen bonds · protein-protein
C–D · 1600 Å² buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 39 modified (engineered).

Compared structures

3DTZ · Crystal structure of Putative Chlorite dismutase TA0507 · 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 Q9HKT8
Elsewhere: RCSB PDB 3DTZ · PDBe 3DTZ · UniProt Q9HKT8

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