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Bacillus subtilis manganese transport regulator (MNTR) bound to manganese, AC conformation, pH 6.5

Analyse Bacillus subtilis manganese transport regulator (MNTR) bound to manganese, AC… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F5D
Type: protein
Length: 261 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.9
Source: Bacillus subtilis
Molecule: Transcriptional regulator mntR
UniProt: P54512
Ligands: MN

Structure

x-ray diffraction · resolution 1.9 · 2 distinct chains · 77% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcriptional regulator mntR	protein	130	78% helix, 3% strand	P54512
B	Transcriptional regulator mntR	protein	131	77% helix, 3% strand	P54512

Ligands and binding sites

MN · Manganese (II) ion · metal · 4 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 1319 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2F5D · Bacillus subtilis manganese transport regulator (mntr) bound to manganese, ac… · the same entry in another collection · chain A against A, TM-score 1.00
P54512 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator mntr (P54512) · 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 P54512
Elsewhere: RCSB PDB 2F5D · PDBe 2F5D · UniProt P54512

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