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1.65A resolution structure of the hypothetical protein CT253 from chlamydia trachomatis

Analyse 1.65A resolution structure of the hypothetical protein CT253 from chlamydia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UXC
Type: protein
Length: 335 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CT253
UniProt: A0A0H3MBU8
Ligands: NA
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CT253	protein	163	39% helix, 29% strand	A0A0H3MBU8
B	CT253	protein	172	33% helix, 27% strand	A0A0H3MBU8

Ligands and binding sites

NA · Sodium ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.41	0.82	16	empty
2	51	0.33	0.78	12	empty
3	57	0.29	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 667 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

6UXC · 1.65A resolution structure of the hypothetical protein CT253 from Chlamydia trachomatis · 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 A0A0H3MBU8
Elsewhere: RCSB PDB 6UXC · PDBe 6UXC · UniProt A0A0H3MBU8

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