MolNFT v1 · #26660 · protein

Crystal structure of trnase Z from thermotoga maritima

1WW1: “Crystal structure of trnase Z from thermotoga maritima”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.52). MolNFT v1 #26660 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1WW1
Type: protein
Length: 488 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
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trnase Z (EC 3.1.26.11)	protein	250	28% helix, 32% strand	Q9WZW8
B	Trnase Z (EC 3.1.26.11)	protein	238	32% helix, 34% strand	Q9WZW8

Ligands and binding sites

ZN · Zinc ion · metal · 2 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	195	0.52	0.77	26	empty
2	212	0.48	0.75	32	ZN
3	66	0.29	0.74	22	ZN

Interfaces

1 interface between chains.

A–B · 1150 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

1WW1 · Crystal structure of tRNase Z from Thermotoga maritima · 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 1WW1 · PDBe 1WW1 · UniProt Q9WZW8

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