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High resolution crystal structure of catalytic domain of chitinase 60 from psychrophilic bacteria moritella marina.
Analyse High resolution crystal structure of catalytic domain of chitinase 60 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4W5Z
- Type
- protein
- Length
- 323 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, CL
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitinase 60 (EC 3.2.1.14) | protein | 323 | 36% helix, 20% strand | B1VBB0 |
Ligands and binding sites
- NA · Sodium ion · metal · 8 copies · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- ACT · Acetate ion · additive · 3 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 236 | 0.53 | 0.76 | 33 | MPD, ACT, CL |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4W5Z · High resolution crystal structure of catalytic domain of Chitinase 60 from psychrophilic… · 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 4W5Z · PDBe 4W5Z · UniProt B1VBB0
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