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Ecorv endonuclease, unliganded, form B

Analyse Ecorv endonuclease, unliganded, form B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AZ3
Type: protein
Length: 401 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ecorv endonuclease
EC: 3.1.21.4
UniProt: P04390
Pockets: 6 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ecorv endonuclease (EC 3.1.21.4)	protein	186	25% helix, 32% strand	P04390
B	Ecorv endonuclease (EC 3.1.21.4)	protein	215	31% helix, 28% strand	P04390

Pockets

6 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	265	0.57	0.77	31	empty
2	132	0.49	0.79	19	empty
3	87	0.47	0.81	19	empty
4	72	0.44	0.81	13	empty
5	173	0.44	0.74	35	empty

Interfaces

1 interface between chains.

A–B · 963 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1AZ3 · Ecorv endonuclease, unliganded, form B · the same entry in another collection · chain A against A, TM-score 1.00
P04390 · AlphaFold monomer V2.0 prediction for type-2 restriction enzyme ecorv (P04390) · 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 P04390
Elsewhere: RCSB PDB 1AZ3 · PDBe 1AZ3 · UniProt P04390

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