MolNFT v1 · #93212 · protein
X-ray structure of the archaeoglobus fulgidus methenyl- tetrahydromethanopterin cyclohydrolase
4GVR · Methenyltetrahydromethanopterin cyclohydrolase: “X-ray structure of the archaeoglobus fulgidus methenyl- tetrahydromethanopterin cyclohydrolase”. X-ray diffraction, 8 pockets (best druggability 0.73). MolNFT v1 #93212 on GenesisL1…
- PDB
- 4GVR
- Type
- protein
- Length
- 945 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methenyltetrahydromethanopterin cyclohydrolase
- EC
- 3.5.4.27
- UniProt
- O28344
- Pockets
- 8 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Methenyltetrahydromethanopterin cyclohydrolase (EC 3.5.4.27) | protein | 315 | 40% helix, 25% strand | O28344 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 876 | 0.73 | 0.77 | 79 | empty |
| 2 | 407 | 0.65 | 0.78 | 33 | empty |
| 3 | 380 | 0.65 | 0.79 | 37 | empty |
| 4 | 358 | 0.62 | 0.78 | 36 | empty |
| 5 | 246 | 0.53 | 0.76 | 31 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1332 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 1332 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 1320 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 4GVR · X-ray structure of the Archaeoglobus fulgidus methenyl-tetrahydromethanopterin… · the same entry in another collection · chain A against A, TM-score 1.00
- O28344 · AlphaFold monomer V2.0 prediction for methenyltetrahydromethanopterin cyclohydrolase… · 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 O28344
- Elsewhere: RCSB PDB 4GVR · PDBe 4GVR · UniProt O28344
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