Research workbench
Crystal structure of hemoglobin I from river lamprey
Analyse Crystal structure of hemoglobin I from river lamprey in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UC3
- Type
- protein
- Length
- 1,788 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Globin
- UniProt
- P02207
- Ligands
- HEM
- Pockets
- 12 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Globin | protein | 149 | 70% helix, 0% strand | P02207 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 997 | 0.85 | 0.85 | 96 | HEM |
| 2 | 974 | 0.85 | 0.85 | 96 | HEM |
| 3 | 819 | 0.82 | 0.84 | 78 | HEM |
| 4 | 1002 | 0.82 | 0.83 | 84 | HEM |
| 5 | 948 | 0.82 | 0.83 | 83 | HEM |
Interfaces
14 interfaces between chains.
- C–D · 511 Ų buried · 15 hydrogen bonds · protein-protein
- K–L · 509 Ų buried · 18 hydrogen bonds · protein-protein
- E–F · 507 Ų buried · 13 hydrogen bonds · protein-protein
- I–J · 503 Ų buried · 15 hydrogen bonds · protein-protein
- G–H · 500 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1UC3 · Crystal Structure of hemoglobin I from river lamprey · the same entry in another collection · chain L against L, 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 P02207
- Elsewhere: RCSB PDB 1UC3 · PDBe 1UC3 · UniProt P02207
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