MolNFT v1 · #35324 · protein

High resolution structure of T. maritima trnase Z

2E7Y: “High resolution structure of T. maritima trnase Z”. X-ray diffraction, 2 ligands (ZN, SO4), 3 pockets (best druggability 0.56). MolNFT v1 #35324 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2E7Y
Type: protein
Length: 541 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Trnase Z
EC: 3.1.26.11
UniProt: Q9WZW8
Ligands: ZN, SO4
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trnase Z (EC 3.1.26.11)	protein	272	36% helix, 30% strand	Q9WZW8
B	Trnase Z (EC 3.1.26.11)	protein	269	33% helix, 30% strand	Q9WZW8

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A
PGO · S-1,2-propanediol · additive · 4 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	214	0.56	0.78	29	PGO
2	220	0.49	0.75	40	empty
3	133	0.44	0.76	25	empty

Interfaces

1 interface between chains.

A–B · 1069 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

2E7Y · High resolution structure of T. maritima tRNase Z · 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 Q9WZW8
Elsewhere: RCSB PDB 2E7Y · PDBe 2E7Y · UniProt Q9WZW8

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