MolNFT v1 · #92245 · protein
Structural and mechanistic basis of substrate recognition by novel di- peptidase DUG1P from saccharomyces cerevisiae
4G1P · Cys-gly metallodipeptidase DUG1: “Structural and mechanistic basis of substrate recognition by novel di- peptidase DUG1P from saccharomyces…”. X-ray diffraction, 1 ligand (ZN), 4 pockets (best druggability 0.70). MolNFT v1 #92245 on…
- PDB
- 4G1P
- Type
- protein
- Length
- 481 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cys-gly metallodipeptidase DUG1
- EC
- 3.4.13.-
- UniProt
- P43616
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cys-gly metallodipeptidase DUG1 (EC 3.4.13.-) | protein | 481 | 36% helix, 21% strand | P43616 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 818 | 0.70 | 0.76 | 87 | empty |
| 2 | 137 | 0.44 | 0.76 | 26 | empty |
| 3 | 53 | 0.28 | 0.74 | 14 | empty |
| 4 | 51 | 0.26 | 0.74 | 16 | empty |
Compared structures
- 4G1P · Structural and Mechanistic Basis of Substrate Recognition by Novel Di-peptidase Dug1p… · the same entry in another collection · chain A against A, TM-score 1.00
- P43616 · AlphaFold monomer V2.0 prediction for cys-gly metallodipeptidase DUG1 (P43616) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P43616
- Elsewhere: RCSB PDB 4G1P · PDBe 4G1P · UniProt P43616
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