MolNFT v1 · #48275 · protein
Crystal structure of human ferrochelatase mutant with his 341 replaced by cys
2PO7 · Ferrochelatase, mitochondrial: “Crystal structure of human ferrochelatase mutant with his 341 replaced by cys”. X-ray diffraction, 2 ligands (CHD, FES), 10 pockets (best druggability 0.80). MolNFT v1 #48275 on GenesisL1: 3D…
- PDB
- 2PO7
- Type
- protein
- Length
- 718 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferrochelatase, mitochondrial
- EC
- 4.99.1.1
- UniProt
- P22830
- Ligands
- CHD, FES
- Pockets
- 10 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ferrochelatase, mitochondrial (EC 4.99.1.1) | protein | 359 | 51% helix, 14% strand | P22830 |
Ligands and binding sites
- CHD · Cholic acid · ligand · 6 copies · chains A, B
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.80 | 0.98 | 34 | empty |
| 2 | 730 | 0.78 | 0.82 | 72 | FES, CHD |
| 3 | 573 | 0.75 | 0.82 | 56 | CHD |
| 4 | 103 | 0.63 | 0.88 | 30 | FES |
| 5 | 225 | 0.54 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1833 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 2PO7 · Crystal structure of human ferrochelatase mutant with His 341 replaced by Cys · the same entry in another collection · chain A against A, TM-score 1.00
- P22830 · AlphaFold monomer V2.0 prediction for ferrochelatase, mitochondrial (P22830) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P22830
- Elsewhere: RCSB PDB 2PO7 · PDBe 2PO7 · UniProt P22830
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