MolNFT v1 · #84323 · protein
Molecular basis for the action of the collagen-specific chaperone HSP47 SERPINH1 and its structure-specific client recognition.
3ZHA: “Molecular basis for the action of the collagen-specific chaperone HSP47 SERPINH1 and its structure-specific…”. X-ray diffraction, 1 ligand (ACE), 20 pockets (best druggability 0.77). MolNFT v1 #84323 on GenesisL1: 3D structure…
- PDB
- 3ZHA
- Type
- protein
- Length
- 3,166 residues
- Chains
- 20
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HSP47; Collagen model peptide 18-T8R11
- UniProt
- C7C419
- Ligands
- ACE
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 11 distinct chains · 31% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HSP47 | protein | 380 | 32% helix, 32% strand | C7C419 |
| B | HSP47 | protein | 364 | 31% helix, 34% strand | C7C419 |
| C | HSP47 | protein | 376 | 32% helix, 34% strand | C7C419 |
| D | HSP47 | protein | 368 | 32% helix, 33% strand | C7C419 |
| E, H, M, N, O, R, S | Collagen model peptide 18-T8R11 | protein | 17 | 0% helix, 0% strand | — |
| F, I, T | Collagen model peptide 18-T8R11 | protein | 16 | 0% helix, 0% strand | — |
| G, J | Collagen model peptide 18-T8R11 | protein | 15 | 0% helix, 0% strand | — |
| K | HSP47 | protein | 374 | 32% helix, 32% strand | C7C419 |
| L | HSP47 | protein | 369 | 31% helix, 33% strand | C7C419 |
| P | HSP47 | protein | 373 | 33% helix, 32% strand | C7C419 |
| Q | HSP47 | protein | 365 | 31% helix, 34% strand | C7C419 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 12 copies · chains E, F, G, A, H, I, J, C, M, N, O, K, R, S, T, P
- SIN · Succinic acid · additive · 5 copies · chains A, C, K, P, Q
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 472 | 0.77 | 0.85 | 56 | empty |
| 2 | 427 | 0.76 | 0.85 | 51 | empty |
| 3 | 741 | 0.76 | 0.81 | 64 | empty |
| 4 | 588 | 0.76 | 0.82 | 46 | empty |
| 5 | 696 | 0.74 | 0.80 | 62 | empty |
Interfaces
43 interfaces between chains.
- A–E · 600 Ų buried · 7 hydrogen bonds · protein-protein
- P–R · 578 Ų buried · 8 hydrogen bonds · protein-protein
- K–M · 570 Ų buried · 6 hydrogen bonds · protein-protein
- C–H · 565 Ų buried · 7 hydrogen bonds · protein-protein
- M–N · 562 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 covalent (covalent ligand).
Compared structures
- 3ZHA · Molecular basis for the action of the collagen-specific chaperone Hsp47 SERPINH1 and its… · 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 C7C419
- Elsewhere: RCSB PDB 3ZHA · PDBe 3ZHA · UniProt C7C419
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