MolNFT v1 · #104453 · protein

1.75 a resolution structure of CT263-D161N (mtan) from chlamydia trachomatis bound to mta

4QAT: “1.75 a resolution structure of CT263-D161N (mtan) from chlamydia trachomatis bound to mta”. X-ray diffraction, 1 ligand (MTA), 5 pockets (best druggability 0.68). MolNFT v1 #104453 on GenesisL1: 3D structure, binding sites and…

PDB: 4QAT
Type: protein
Length: 384 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CT263
UniProt: B0B7H9
Ligands: MTA
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CT263	protein	195	24% helix, 35% strand	B0B7H9
B	CT263	protein	189	26% helix, 34% strand	B0B7H9

Ligands and binding sites

MTA · 5'-deoxy-5'-methylthioadenosine · ligand · chains B

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

Pockets

5 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	416	0.68	0.80	45	empty
2	204	0.67	0.85	24	MTA
3	208	0.62	0.82	35	empty
4	53	0.31	0.76	10	empty
5	52	0.24	0.72	14	empty

Interfaces

1 interface between chains.

A–B · 757 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4QAT · 1.75 A resolution structure of CT263-D161N (MTAN) from Chlamydia trachomatis bound to MTA · 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 4QAT · PDBe 4QAT · UniProt B0B7H9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.