Research workbench
Crystal structure of a double mutant (C202A and C222D) of triosephosphate isomerase from giardia lamblia.
Analyse Crystal structure of a double mutant (C202A and C222D) of triosephosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BI5
- Type
- protein
- Length
- 5,080 residues
- Chains
- 20
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- P36186
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T | Triosephosphate isomerase (EC 5.3.1.1) | protein | 254 | 49% helix, 15% strand | P36186 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 836 | 0.82 | 0.84 | 88 | empty |
| 2 | 921 | 0.80 | 0.82 | 95 | empty |
| 3 | 1096 | 0.79 | 0.80 | 103 | empty |
| 4 | 1026 | 0.77 | 0.79 | 98 | empty |
| 5 | 110 | 0.77 | 0.97 | 29 | empty |
Interfaces
40 interfaces between chains.
- S–T · 1513 Ų buried · 31 hydrogen bonds · protein-protein
- M–N · 1507 Ų buried · 26 hydrogen bonds · protein-protein
- K–L · 1503 Ų buried · 21 hydrogen bonds · protein-protein
- E–F · 1494 Ų buried · 23 hydrogen bonds · protein-protein
- Q–R · 1488 Ų buried · 29 hydrogen bonds · protein-protein
Compared structures
- 4BI5 · Crystal structure of a double mutant (C202A and C222D) of triosephosphate isomerase from… · the same entry in another collection · chain T against T, 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 P36186
- Elsewhere: RCSB PDB 4BI5 · PDBe 4BI5 · UniProt P36186
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