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1.45 a resolution structure of CT263 (mtan) from chlamydia trachomatis bound to adenine

Analyse 1.45 a resolution structure of CT263 (mtan) from chlamydia trachomatis bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QAR
Type: protein
Length: 382 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CT263
UniProt: B0B7H9
Ligands: ADE, SO4
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CT263	protein	195	24% helix, 34% strand	B0B7H9
B	CT263	protein	187	27% helix, 34% strand	B0B7H9

Ligands and binding sites

ADE · Adenine · ligand · chains B
SO4 · Sulfate ion · ion · chains A

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

Pockets

4 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	536	0.71	0.80	53	empty
2	207	0.61	0.82	28	empty
3	164	0.56	0.81	23	ADE
4	64	0.37	0.78	13	empty

Interfaces

1 interface between chains.

A–B · 670 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

4QAR · 1.45 A resolution structure of CT263 (MTAN) from Chlamydia trachomatis bound to Adenine · 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 B0B7H9
Elsewhere: RCSB PDB 4QAR · PDBe 4QAR · UniProt B0B7H9

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