MolNFT v1 · #109311 · protein

Crystal structure of human translin in open conformation

4WYV: “Crystal structure of human translin in open conformation”. X-ray diffraction, 20 pockets (best druggability 0.73). MolNFT v1 #109311 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4WYV
Type: protein
Length: 1,702 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Translin
EC: 3.1.-.-
UniProt: Q15631
Pockets: 20 · best druggability 0.73

Structure

x-ray diffraction · 7 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Translin (EC 3.1.-.-)	protein	213	83% helix, 0% strand	Q15631
B, F	Translin (EC 3.1.-.-)	protein	212	82% helix, 0% strand	Q15631
C	Translin (EC 3.1.-.-)	protein	210	82% helix, 0% strand	Q15631
D	Translin (EC 3.1.-.-)	protein	214	82% helix, 0% strand	Q15631
E	Translin (EC 3.1.-.-)	protein	213	82% helix, 0% strand	Q15631
G	Translin (EC 3.1.-.-)	protein	216	78% helix, 0% strand	Q15631
H	Translin (EC 3.1.-.-)	protein	212	82% helix, 0% strand	Q15631

Pockets

20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	633	0.73	0.80	45	empty
2	519	0.68	0.79	40	empty
3	598	0.68	0.77	38	empty
4	720	0.68	0.76	44	empty
5	576	0.68	0.77	40	empty

Interfaces

16 interfaces between chains.

C–G · 1721 Å² buried · 12 hydrogen bonds · protein-protein
A–E · 1685 Å² buried · 12 hydrogen bonds · protein-protein
B–F · 1621 Å² buried · 10 hydrogen bonds · protein-protein
D–H · 1606 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 795 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4WYV · Crystal Structure of Human Translin in Open Conformation · the same entry in another collection · chain H against H, TM-score 1.00
Q15631 · AlphaFold monomer V2.0 prediction for translin (Q15631) · 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 Q15631
Elsewhere: RCSB PDB 4WYV · PDBe 4WYV · UniProt Q15631

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