MolNFT v1 · #4156 · protein
The crystal structure of modified bovine fibrinogen (at ~4 ångström resolution)
1DEQ · Fibrinogen (alpha chain): “The crystal structure of modified bovine fibrinogen (at ~4 ångström resolution)”. X-ray diffraction, 13 pockets (best druggability 0.34). MolNFT v1 #4156 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1DEQ
- Type
- protein
- Length
- 3,900 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibrinogen (alpha chain); Fibrinogen (beta chain); Fibrinogen (gamma chain); Fibrinogen
- UniProt
- P02672, P02676, P12799
- Pockets
- 13 · best druggability 0.34
Structure
x-ray diffraction · 4 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, N, Q | Fibrinogen (alpha chain) | protein | 180 | 0% helix, 0% strand | P02672 |
| B, E, O, R | Fibrinogen (beta chain) | protein | 380 | 0% helix, 0% strand | P02676 |
| C, F, P, S | Fibrinogen (gamma chain) | protein | 370 | 0% helix, 0% strand | P12799 |
| M, Z | Fibrinogen | protein | 90 | 0% helix, 0% strand | — |
Pockets
13 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.34 | 0.73 | 19 | empty |
| 2 | 78 | 0.34 | 0.73 | 23 | empty |
| 3 | 66 | 0.33 | 0.74 | 26 | empty |
| 4 | 73 | 0.33 | 0.73 | 26 | empty |
| 5 | 70 | 0.32 | 0.73 | 21 | empty |
Interfaces
25 interfaces between chains.
- O–P · 294 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 267 Ų buried · 0 hydrogen bonds · protein-protein
- E–F · 242 Ų buried · 0 hydrogen bonds · protein-protein
- Q–R · 232 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 217 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1DEQ · The crystal structure of modified bovine fibrinogen (at ~4 ångström resolution) · the same entry in another collection · chain F against F, 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 P02672
- Every structure of UniProt P02676
- Every structure of UniProt P12799
- Elsewhere: RCSB PDB 1DEQ · PDBe 1DEQ · UniProt P02672 · UniProt P02676 · UniProt P12799
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