Research workbench
Human methemoglobin state 1 determined using single-particle cryo-EM at 200 kev
Analyse Human methemoglobin state 1 determined using single-particle cryo-EM at 200 kev in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NBC
- Type
- protein
- Length
- 566 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin subunit alpha; Hemoglobin subunit beta
- UniProt
- P69905, P68871
- Ligands
- HEM
- Pockets
- 7 · best druggability 0.86
Structure
electron microscopy · 2 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Hemoglobin subunit alpha | protein | 140 | 79% helix, 0% strand | P69905 |
| B, D | Hemoglobin subunit beta | protein | 143 | 78% helix, 0% strand | P68871 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 888 | 0.86 | 0.87 | 116 | empty |
| 2 | 223 | 0.74 | 0.88 | 27 | HEM |
| 3 | 229 | 0.73 | 0.87 | 30 | HEM |
| 4 | 188 | 0.68 | 0.86 | 25 | HEM |
| 5 | 177 | 0.68 | 0.86 | 25 | HEM |
Interfaces
5 interfaces between chains.
- C–D · 952 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 939 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 474 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 472 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 383 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6NBC · human methemoglobin state 1 determined using single-particle cryo-EM at 200 keV · 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 P69905
- Every structure of UniProt P68871
- Elsewhere: RCSB PDB 6NBC · PDBe 6NBC · UniProt P69905 · UniProt P68871
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