Research workbench

Crystal structure of np exonuclease C409A-pcmps complex

Analyse Crystal structure of np exonuclease C409A-pcmps complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7V3B
Type: protein
Length: 414 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoprotein
EC: 3.1.13.-
UniProt: P13699
Ligands: PMB, MG, ZN
Pockets: 7 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Nucleoprotein (EC 3.1.13.-)	protein	207	36% helix, 23% strand	P13699

Ligands and binding sites

PMB · Para-mercury-benzenesulfonic acid · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A, B
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

7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	161	0.49	0.78	23	MG
2	164	0.48	0.77	19	empty
3	65	0.43	0.82	17	empty
4	156	0.42	0.74	17	MG
5	137	0.42	0.75	26	empty

Interfaces

1 interface between chains.

A–B · 438 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

7V3B · Crystal structure of NP exonuclease C409A-PCMPS complex · 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 P13699
Elsewhere: RCSB PDB 7V3B · PDBe 7V3B · UniProt P13699

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