MolNFT v1 · #13963 · protein
Crystal structure of recombinant human fibrinogen fragment D with the peptide ligands gly-pro-arg-pro-amide and gly-his-arg-pro-amide
1LTJ · Fibrinogen ALPHA/ALPHA-E chain: “Crystal structure of recombinant human fibrinogen fragment D with the peptide ligands gly-pro-arg-pro-amide…”. X-ray diffraction, 3 ligands (NAG, FUC, CA), 15 pockets (best druggability 0.62). MolNFT…
- PDB
- 1LTJ
- Type
- protein
- Length
- 1,315 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibrinogen ALPHA/ALPHA-E chain; Fibrinogen beta chain; Fibrinogen gamma chain…
- UniProt
- P02671, P02675, P02679
- Ligands
- NAG, FUC, CA
- Pockets
- 15 · best druggability 0.62
Structure
x-ray diffraction · 8 distinct chains · 26% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibrinogen ALPHA/ALPHA-E chain | protein | 65 | 69% helix, 2% strand | P02671 |
| B | Fibrinogen beta chain | protein | 298 | 22% helix, 27% strand | P02675 |
| C | Fibrinogen gamma chain | protein | 299 | 23% helix, 24% strand | P02679 |
| D | Fibrinogen ALPHA/ALPHA-E chain | protein | 58 | 60% helix, 2% strand | P02671 |
| E | Fibrinogen beta chain | protein | 294 | 24% helix, 27% strand | P02675 |
| F | Fibrinogen gamma chain | protein | 285 | 20% helix, 26% strand | P02679 |
| G, I | Gly-pro-arg-pro | protein | 4 | 0% helix, 25% strand | — |
| H, J | Gly-his-arg-pro | protein | 4 | 0% helix, 25% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains B, H, E, J
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains B, H, J
- CA · Calcium ion · metal · 4 copies · chains B, C, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.62 | 0.84 | 26 | empty |
| 2 | 163 | 0.62 | 0.84 | 26 | empty |
| 3 | 211 | 0.60 | 0.81 | 35 | empty |
| 4 | 197 | 0.59 | 0.81 | 33 | empty |
| 5 | 283 | 0.57 | 0.77 | 36 | empty |
Interfaces
10 interfaces between chains.
- B–C · 2155 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1916 Ų buried · 26 hydrogen bonds · protein-protein
- E–F · 1871 Ų buried · 22 hydrogen bonds · protein-protein
- D–E · 1739 Ų buried · 26 hydrogen bonds · protein-protein
- A–C · 878 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 1LTJ · Crystal Structure of Recombinant Human Fibrinogen Fragment D with the Peptide Ligands… · the same entry in another collection · chain J against J, TM-score 1.00
- P02675 · AlphaFold monomer V2.0 prediction for fibrinogen beta chain (P02675) · a predicted model of the same protein · chain E against A, TM-score 0.99
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 P02671
- Every structure of UniProt P02675
- Every structure of UniProt P02679
- Elsewhere: RCSB PDB 1LTJ · PDBe 1LTJ · UniProt P02671 · UniProt P02675 · UniProt P02679
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