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Brucella melitensis nrnc with bound MG2+

Analyse Brucella melitensis nrnc with bound MG2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MPT
Type: protein
Length: 407 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: MG, PO4
Pockets: 6 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 42% 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	201	41% helix, 17% strand	A0A2X1C2S7

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains A, B
PO4 · Phosphate ion · ion · chains B

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

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	306	0.54	0.75	27	MG
2	121	0.44	0.77	18	empty
3	104	0.41	0.77	22	empty
4	139	0.41	0.74	19	MG
5	69	0.32	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 477 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7MPT · Brucella melitensis NrnC with bound Mg2+ · 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 7MPT · PDBe 7MPT · UniProt A0A2X1C2S7

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