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Crystal structure of human PCNA in complex with parg (POLY(ADP-ribose) glycohydrolase) peptide.
Analyse Crystal structure of human PCNA in complex with parg (POLY(ADP-ribose)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MAV
- Type
- protein
- Length
- 1,574 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proliferating cell nuclear antigen; Poly (ADP-ribose) glycohydrolase
- UniProt
- P12004, Q0MQR4
- Pockets
- 14 · best druggability 0.76
Structure
x-ray diffraction · 10 distinct chains · 19% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proliferating cell nuclear antigen | protein | 254 | 20% helix, 47% strand | P12004 |
| C, E | Proliferating cell nuclear antigen | protein | 251 | 19% helix, 47% strand | P12004 |
| B | Proliferating cell nuclear antigen | protein | 253 | 20% helix, 45% strand | P12004 |
| D | Proliferating cell nuclear antigen | protein | 243 | 20% helix, 44% strand | P12004 |
| F | Proliferating cell nuclear antigen | protein | 250 | 19% helix, 48% strand | P12004 |
| G | Poly (ADP-ribose) glycohydrolase | protein | 14 | 21% helix, 14% strand | Q0MQR4 |
| H | Poly (ADP-ribose) glycohydrolase | protein | 13 | 23% helix, 23% strand | Q0MQR4 |
| K, M | Poly (ADP-ribose) glycohydrolase | protein | 12 | 25% helix, 17% strand | Q0MQR4 |
| L | Poly (ADP-ribose) glycohydrolase | protein | 11 | 0% helix, 18% strand | Q0MQR4 |
| N | Poly (ADP-ribose) glycohydrolase | protein | 10 | 30% helix, 10% strand | Q0MQR4 |
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.76 | 0.91 | 30 | empty |
| 2 | 51 | 0.74 | 0.99 | 18 | empty |
| 3 | 833 | 0.72 | 0.77 | 80 | empty |
| 4 | 443 | 0.57 | 0.74 | 41 | empty |
| 5 | 215 | 0.56 | 0.79 | 29 | empty |
Interfaces
17 interfaces between chains.
- B–D · 793 Ų buried · 13 hydrogen bonds · protein-protein
- A–H · 769 Ų buried · 9 hydrogen bonds · protein-protein
- C–G · 767 Ų buried · 9 hydrogen bonds · protein-protein
- B–K · 744 Ų buried · 11 hydrogen bonds · protein-protein
- B–F · 742 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5MAV · Crystal structure of human PCNA in complex with PARG (poly(ADP-ribose) glycohydrolase)… · 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 P12004
- Every structure of UniProt Q0MQR4
- Elsewhere: RCSB PDB 5MAV · PDBe 5MAV · UniProt P12004 · UniProt Q0MQR4
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