MolNFT v1 · #88758 · protein

Crystal structure of KTI13/ATS1

4D4Q · Protein ATS1: “Crystal structure of KTI13/ATS1”. X-ray diffraction, 9 pockets (best druggability 0.75). MolNFT v1 #88758 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4D4Q
Type: protein
Length: 648 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein ATS1
UniProt: P31386
Pockets: 9 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein ATS1	protein	329	1% helix, 48% strand	P31386
B	Protein ATS1	protein	319	1% helix, 47% strand	P31386

Pockets

9 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	527	0.75	0.83	46	empty
2	569	0.75	0.82	49	empty
3	121	0.55	0.83	29	empty
4	266	0.55	0.76	23	empty
5	89	0.50	0.83	21	empty

Interfaces

1 interface between chains.

A–B · 580 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

4D4Q · Crystal Structure of Kti13/AtS1 · the same entry in another collection · chain A against A, TM-score 1.00
P31386 · AlphaFold monomer V2.0 prediction for protein KTI13 (P31386) · a predicted model of the same protein · chain B 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 P31386
Elsewhere: RCSB PDB 4D4Q · PDBe 4D4Q · UniProt P31386

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