Research workbench
Crystal structure of an truncated transition metal transporter
Analyse Crystal structure of an truncated transition metal transporter in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M5B
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cobalamin biosynthesis protein cbim
- UniProt
- Q8R9C0
- Ligands
- NI
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cobalamin biosynthesis protein cbim | protein | 214 | 74% helix, 3% strand | Q8R9C0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4M5B · Crystal Structure of an Truncated Transition Metal Transporter · 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 Q8R9C0
- Elsewhere: RCSB PDB 4M5B · PDBe 4M5B · UniProt Q8R9C0
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