MolNFT v1 · #3110 · protein
Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures
1CHM: “Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures”. X-ray diffraction, 1 ligand (CMS), 8 pockets (best druggability 0.86). MolNFT v1 #3110 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1CHM
- Type
- protein
- Length
- 802 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Creatine amidinohydrolase
- EC
- 3.5.3.3
- UniProt
- P38488
- Ligands
- CMS
- Pockets
- 8 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Creatine amidinohydrolase (EC 3.5.3.3) | protein | 401 | 37% helix, 24% strand | P38488 |
Ligands and binding sites
- CMS · Carbamoyl sarcosine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 397 | 0.86 | 0.94 | 49 | empty |
| 2 | 1002 | 0.86 | 0.87 | 92 | empty |
| 3 | 69 | 0.58 | 0.89 | 25 | empty |
| 4 | 130 | 0.49 | 0.79 | 18 | empty |
| 5 | 85 | 0.48 | 0.82 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 3393 Ų buried · 46 hydrogen bonds · protein-protein
Compared structures
- 1CHM · Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures · the same entry in another collection · chain A against A, TM-score 1.00
- P38488 · AlphaFold monomer V2.0 prediction for creatinase (P38488) · a predicted model of the same protein · 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 P38488
- Elsewhere: RCSB PDB 1CHM · PDBe 1CHM · UniProt P38488
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