Research workbench
Crystal structure of medicago truncatula (DELTA)1-pyrroline-5- carboxylate reductase (MTP5CR) in complex with L-proline
Analyse Crystal structure of medicago truncatula (DELTA)1-pyrroline-5- carboxylate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BSH
- Type
- protein
- Length
- 2,700 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyrroline-5-carboxylate reductase
- EC
- 1.5.1.2
- UniProt
- G7KRM5
- Ligands
- PRO
- Pockets
- 20 · best druggability 0.71
Structure
x-ray diffraction · 5 distinct chains · 58% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E, F, H | Pyrroline-5-carboxylate reductase (EC 1.5.1.2) | protein | 272 | 57% helix, 13% strand | G7KRM5 |
| C, D | Pyrroline-5-carboxylate reductase (EC 1.5.1.2) | protein | 268 | 58% helix, 13% strand | G7KRM5 |
| G | Pyrroline-5-carboxylate reductase (EC 1.5.1.2) | protein | 263 | 59% helix, 13% strand | G7KRM5 |
| I | Pyrroline-5-carboxylate reductase (EC 1.5.1.2) | protein | 270 | 58% helix, 13% strand | G7KRM5 |
| J | Pyrroline-5-carboxylate reductase (EC 1.5.1.2) | protein | 271 | 57% helix, 13% strand | G7KRM5 |
Ligands and binding sites
- PRO · Proline · ligand · 10 copies · chains A, B, C, D, E, F, G, H, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 766 | 0.71 | 0.77 | 64 | PRO |
| 2 | 562 | 0.68 | 0.78 | 46 | PRO |
| 3 | 596 | 0.68 | 0.77 | 50 | PRO |
| 4 | 579 | 0.67 | 0.77 | 43 | PRO |
| 5 | 545 | 0.66 | 0.77 | 42 | PRO |
Interfaces
25 interfaces between chains.
- I–J · 4222 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 4216 Ų buried · 16 hydrogen bonds · protein-protein
- G–H · 4204 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 4200 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 4193 Ų buried · 15 hydrogen bonds · protein-protein
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 G7KRM5
- Elsewhere: RCSB PDB 5BSH · PDBe 5BSH · UniProt G7KRM5
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