MolNFT v1 · #85934 · protein
Crystal structure of the collagenase unit of collagenase G from clostridium histolyticum at 2.19 ångström resolution.
4ARE: “Crystal structure of the collagenase unit of collagenase G from clostridium histolyticum at 2.19 ångström…”. X-ray diffraction, 1 ligand (ZN), 6 pockets (best druggability 0.51). MolNFT v1 #85934 on GenesisL1: 3D structure, binding…
- PDB
- 4ARE
- Type
- protein
- Length
- 678 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagenase G
- EC
- 3.4.24.3
- UniProt
- Q9X721
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagenase G (EC 3.4.24.3) | protein | 678 | 56% helix, 11% strand | Q9X721 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- P6G · Hexaethylene glycol · additive · chains A
- FLC · Citrate anion · additive · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.51 | 0.80 | 24 | empty |
| 2 | 207 | 0.47 | 0.74 | 36 | empty |
| 3 | 61 | 0.45 | 0.83 | 15 | empty |
| 4 | 111 | 0.36 | 0.73 | 21 | empty |
| 5 | 94 | 0.36 | 0.74 | 18 | FLC |
Compared structures
- 4ARE · Crystal structure of the collagenase Unit of collagenase G from Clostridium histolyticum… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X721 · AlphaFold monomer V2.0 prediction for collagenase colg (Q9X721) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9X721
- Elsewhere: RCSB PDB 4ARE · PDBe 4ARE · UniProt Q9X721
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