Research workbench
Crystal structure of fragment double-D from human fibrin with the peptide ligand gly-his-arg-pro-amide
Analyse Crystal structure of fragment double-D from human fibrin with the peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FZF
- Type
- protein
- Length
- 1,313 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02671, P02675, P02679
Structure
x-ray diffraction · 7 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 67 | — | P02671 |
| B | — | protein | 303 | — | P02675 |
| C | — | protein | 292 | — | P02679 |
| D | — | protein | 54 | — | P02671 |
| E | — | protein | 296 | — | P02675 |
| F | — | protein | 285 | — | P02679 |
| S, T, M, N | — | protein | 4 | — | P02675 |
Compared structures
- 1FZF · Crystal structure of fragment double-D from human fibrin with the peptide ligand… · the same entry in another collection · chain N against N, 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 1FZF · PDBe 1FZF · UniProt P02671 · UniProt P02675 · UniProt P02679
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