1JY2: Central Region of Bovine Fibrinogen
Crystal Structure of the Central Region of Bovine Fibrinogen (E5 fragment) at 1.4 Angstroms Resolution. Determined by X-ray diffraction at 1.4 Å resolution. Released 17 Oct 2001.
- Method
- X-ray diffraction
- Resolution
- 1.4 Å
- Organism
- Bos taurus
- Chains
- 6
- Atoms
- 2,514
- Mol. weight
- 35.8 kDa
- Released
- 17 Oct 2001
Explore 1JY2 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1JY2 contains 15 α-helices and 15 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain N: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 36-37 | 2 | |
| β-strand | 38 | 1 | 1 |
| α-helix | 39 | 1 | |
| α-helix | 41-43 | 3 | |
| β-strand | 44 | 1 | 1 |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 51-76 | 26 | |
Chain O: 2 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-67 | 3 | |
| β-strand | 72-73 | 2 | 2 |
| β-strand | 81-82 | 2 | 2 |
| β-strand | 83-84 | 2 | 3 |
| α-helix | 86-112 | 27 | |
Chain P: 1 helix, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12 | 1 | 4 |
| β-strand | 16 | 1 | 4 |
| β-strand | 18-20 | 3 | 5 |
| α-helix | 22-47 | 26 | |
Chain Q: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 36-37 | 2 | |
| β-strand | 38 | 1 | 2 |
| α-helix | 39 | 1 | |
| α-helix | 41-43 | 3 | |
| β-strand | 44 | 1 | 3 |
| β-strand | 47-48 | 2 | 3 |
| α-helix | 51-76 | 26 | |
Chain R: 2 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-67 | 3 | |
| β-strand | 72-73 | 2 | 1 |
| β-strand | 81-84 | 4 | 1 |
| α-helix | 86-111 | 26 | |
Chain S: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-15 | 3 | |
| β-strand | 18-20 | 3 | 5 |
| α-helix | 22-47 | 26 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Fibrinogen alpha chain | N, Q | protein | 53 | Bos taurus | P02672 (AlphaFold model) |
| Fibrinogen beta chain | O, R | protein | 56 | Bos taurus | P02676 (AlphaFold model) |
| Fibrinogen gamma-B chain | P, S | protein | 48 | Bos taurus | P12799 (AlphaFold model) |
Sequence of entity 1 (N, Q), FASTA
>1JY2_1 FIBRINOGEN ALPHA CHAIN (chains N, Q)
SACKETGWPFCSDEDWNTKCPSGCRMKGLIDEVDQDFTSRINKLRDSLFNYQK
Sequence of entity 2 (O, R), FASTA
>1JY2_2 FIBRINOGEN BETA CHAIN (chains O, R)
KVERKPPDADGCLHADPDLGVLCPTGCKLQDTLVRQERPIRKSIEDLRNTVDSVSR
Sequence of entity 3 (P, S), FASTA
>1JY2_3 FIBRINOGEN GAMMA-B CHAIN (chains P, S)
YVATRDNCCILDERFGSYCPTTCGIADFLNNYQTSVDKDLRTLEGILY
Primary citation
Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution. Madrazo, J., Brown, J.H., Litvinovich, S. et al. Proc Natl Acad Sci U S A (2001) 98:11967-11972. DOI 10.1073/pnas.211439798 · PubMed
Other PDB entries of the same protein (UniProt P02672 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1JY3 1.6 Å, Crystal Structure of the Central Region of Bovine Fibrinogen (E5 Fragment) at 1.4…
- 1DEQ 3.5 Å, The crystal structure of modified bovine fibrinogen (at ~4 Å resolution)
- 2BAF Bovine Fibrinogen alpha-C Domain
- 2JOR NMR Solution Structure, Stability, and Interaction of the Recombinant Bovine Fibrinogen…
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