Research workbench

Brucella melitensis nrnc

Analyse Brucella melitensis nrnc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MPR
Type: protein
Length: 410 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nanornase C
EC: 3.1.13.5
UniProt: A0A2X1C2S7
Ligands: SO4
Pockets: 9 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nanornase C (EC 3.1.13.5)	protein	206	42% helix, 16% strand	A0A2X1C2S7
B	Nanornase C (EC 3.1.13.5)	protein	204	41% helix, 17% strand	A0A2X1C2S7

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	330	0.55	0.75	26	empty
2	249	0.54	0.77	31	empty
3	121	0.43	0.76	21	empty
4	107	0.40	0.76	20	empty
5	51	0.36	0.80	16	empty

Interfaces

1 interface between chains.

A–B · 474 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7MPR · Brucella melitensis NrnC · 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 A0A2X1C2S7
Elsewhere: RCSB PDB 7MPR · PDBe 7MPR · UniProt A0A2X1C2S7

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