Research workbench
High-resolution solid-state NMR structure of a 17.6 kda protein
Analyse High-resolution solid-state NMR structure of a 17.6 kda protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KRJ
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Macrophage metalloelastase
- EC
- 3.4.24.65
- UniProt
- P39900
- Ligands
- CO
- Pockets
- 2 · best druggability 0.50
Structure
solid-state nmr · 1 distinct chain · 22% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Macrophage metalloelastase (EC 3.4.24.65) | protein | 152 | 22% helix, 11% strand | P39900 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.50 | 0.83 | 21 | empty |
| 2 | 77 | 0.35 | 0.76 | 15 | empty |
Compared structures
- 2KRJ · High-Resolution Solid-State NMR Structure of a 17.6 kDa Protein · the same entry in another collection · chain A against A, 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 P39900
- Elsewhere: RCSB PDB 2KRJ · PDBe 2KRJ · UniProt P39900
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