Research workbench
Structure of the mntr FE2+ complex with E site metal binding
Analyse Structure of the mntr FE2+ complex with E site metal binding in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HV5
- Type
- protein
- Length
- 253 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P54512
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 126 | — | P54512 |
| B | — | protein | 127 | — | P54512 |
Compared structures
- 4HV5 · Structure of the MNTR FE2+ complex with E site metal binding · 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 A 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 4HV5 · PDBe 4HV5 · UniProt P54512
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