Research workbench
Trimeric human arginase 1 in complex with MAB1 - 2 HARG:3 MAB1 complex
Analyse Trimeric human arginase 1 in complex with MAB1 - 2 HARG:3 MAB1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LEX
- Type
- protein
- Length
- 4,554 residues
- Chains
- 18
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arginase-1; MAB1 heavy chain; MAB1 light chain
- EC
- 3.5.3.1
- UniProt
- P05089
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 3 distinct chains · 17% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, J, M, N | Arginase-1 (EC 3.5.3.1) | protein | 317 | 37% helix, 14% strand | P05089 |
| D, F, G, K, Q, R | MAB1 heavy chain | protein | 228 | 0% helix, 38% strand | — |
| E, H, I, L, O, P | MAB1 light chain | protein | 214 | 6% helix, 38% strand | — |
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 | 1100 | 0.86 | 0.87 | 111 | empty |
| 2 | 669 | 0.83 | 0.88 | 66 | empty |
| 3 | 659 | 0.83 | 0.88 | 62 | empty |
| 4 | 674 | 0.83 | 0.87 | 70 | empty |
| 5 | 606 | 0.83 | 0.88 | 65 | empty |
Interfaces
33 interfaces between chains.
- D–E · 1909 Ų buried · 25 hydrogen bonds · protein-protein
- I–G · 1897 Ų buried · 25 hydrogen bonds · protein-protein
- L–K · 1896 Ų buried · 25 hydrogen bonds · protein-protein
- P–R · 1896 Ų buried · 25 hydrogen bonds · protein-protein
- O–Q · 1882 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 disulfide (disulfide).
Compared structures
- 7LEX · Trimeric human Arginase 1 in complex with mAb1 - 2 hArg:3 mAb1 complex · the same entry in another collection · chain R against R, 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 P05089
- Elsewhere: RCSB PDB 7LEX · PDBe 7LEX · UniProt P05089
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