MolNFT v1 · #69011 · protein
Cofactor-independent phosphoglycerate mutase from thermoplasma acidophilum dsm 1728
3KD8 · 2,3-bisphosphoglycerate-independent phosphoglycerate mutase: “Cofactor-independent phosphoglycerate mutase from thermoplasma acidophilum dsm 1728”. X-ray diffraction, 3 pockets (best druggability 0.74). MolNFT v1 #69011 on…
- PDB
- 3KD8
- Type
- protein
- Length
- 732 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- EC
- 5.4.2.1
- UniProt
- Q9HL27
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (EC 5.4.2.1) | protein | 367 | 34% helix, 24% strand | Q9HL27 |
| B | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (EC 5.4.2.1) | protein | 365 | 35% helix, 23% strand | Q9HL27 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1111 | 0.74 | 0.77 | 103 | empty |
| 2 | 103 | 0.51 | 0.82 | 26 | empty |
| 3 | 51 | 0.41 | 0.82 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 167 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 26 modified, 2 disulfide (engineered, disulfide).
Compared structures
- 3KD8 · Cofactor-Independent Phosphoglycerate mutase from Thermoplasma Acidophilum DSM 1728 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HL27 · AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- independent… · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q9HL27
- Elsewhere: RCSB PDB 3KD8 · PDBe 3KD8 · UniProt Q9HL27
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