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Structure of the mntr FE2+ complex

Analyse Structure of the mntr FE2+ complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3R60
Type: protein
Length: 269 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional regulator mntr
UniProt: P54512
Ligands: FE2

Structure

x-ray diffraction · 2 distinct chains · 76% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcriptional regulator mntr	protein	136	75% helix, 6% strand	P54512
B	Transcriptional regulator mntr	protein	133	77% helix, 5% strand	P54512

Ligands and binding sites

FE2 · Fe (II) ion · metal · 2 copies · chains A, B
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B
PGO · S-1,2-propanediol · additive · chains B

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

Interfaces

1 interface between chains.

A–B · 1337 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

3R60 · Structure of the MntR Fe2+ Complex · 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 0.96

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 3R60 · PDBe 3R60 · UniProt P54512

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