MolNFT v1 · #31930 · protein
Structure of human transcobalamin in complex with cobalamin
2BB5 · Transcobalamin II: “Structure of human transcobalamin in complex with cobalamin”. X-ray diffraction, 1 ligand (B12), 5 pockets (best druggability 0.79). MolNFT v1 #31930 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2BB5
- Type
- protein
- Length
- 818 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcobalamin II
- UniProt
- P20062
- Ligands
- B12
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transcobalamin II | protein | 409 | 45% helix, 12% strand | P20062 |
Ligands and binding sites
- B12 · Cobalamin · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1089 | 0.79 | 0.80 | 64 | B12 |
| 2 | 1122 | 0.78 | 0.80 | 66 | B12 |
| 3 | 668 | 0.67 | 0.76 | 71 | empty |
| 4 | 189 | 0.52 | 0.78 | 31 | empty |
| 5 | 52 | 0.31 | 0.77 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 479 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 P20062
- Elsewhere: RCSB PDB 2BB5 · PDBe 2BB5 · UniProt P20062
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