Research workbench
Crystal structure of cold-adapted chitinase from moritella marina
Analyse Crystal structure of cold-adapted chitinase from moritella marina in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HMC
- Type
- protein
- Length
- 528 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitinase 60
- EC
- 3.2.1.14
- UniProt
- B1VBB0
- Ligands
- NA
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitinase 60 (EC 3.2.1.14) | protein | 528 | 24% helix, 30% strand | B1VBB0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 245 | 0.55 | 0.78 | 33 | empty |
| 2 | 248 | 0.53 | 0.76 | 31 | empty |
| 3 | 116 | 0.40 | 0.76 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4HMC · Crystal structure of cold-adapted chitinase from Moritella marina · 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 B1VBB0
- Elsewhere: RCSB PDB 4HMC · PDBe 4HMC · UniProt B1VBB0
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