MolNFT v1 · #14326 · protein
FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN fromyltransferase from methanosarcina barkeri
1M5S · Formylmethanofuran--tetrahydromethanopterin…: “FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN fromyltransferase from methanosarcina barkeri”. X-ray diffraction, 11 pockets (best druggability 0.76). MolNFT v1 #14326 on GenesisL1: 3D…
- PDB
- 1M5S
- Type
- protein
- Length
- 1,188 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Formylmethanofuran--tetrahydromethanopterin formyltransferase
- EC
- 2.3.1.101
- UniProt
- P55301
- Pockets
- 11 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Formylmethanofuran--tetrahydromethanopterin formyltransferase (EC 2.3.1.101) | protein | 297 | 28% helix, 34% strand | P55301 |
Pockets
11 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 519 | 0.76 | 0.83 | 51 | empty |
| 2 | 596 | 0.75 | 0.82 | 58 | empty |
| 3 | 510 | 0.75 | 0.83 | 52 | empty |
| 4 | 507 | 0.75 | 0.83 | 57 | empty |
| 5 | 553 | 0.75 | 0.82 | 57 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3048 Ų buried · 52 hydrogen bonds · protein-protein
- A–B · 3045 Ų buried · 50 hydrogen bonds · protein-protein
- B–C · 709 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 699 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 336 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1M5S · Formylmethanofuran:tetrahydromethanopterin fromyltransferase from Methanosarcina barkeri · the same entry in another collection · chain C against C, TM-score 1.00
- P55301 · AlphaFold monomer V2.0 prediction for formylmethanofuran-- tetrahydromethanopterin… · a predicted model of the same protein · chain C 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 P55301
- Elsewhere: RCSB PDB 1M5S · PDBe 1M5S · UniProt P55301
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