Research workbench
Crystal structure of deuterated gamma-chymotrypsin at pH 9, cryo temperature
Analyse Crystal structure of deuterated gamma-chymotrypsin at pH 9, cryo temperature in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5R4B
- Type
- protein
- Length
- 247 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-chymotrypsin; Peptide swpw; Peptide tpgvy
- EC
- 3.4.21.1
- UniProt
- P00766
- Ligands
- SO4, IOD
Structure
x-ray diffraction · 5 distinct chains · 11% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-chymotrypsin (EC 3.4.21.1) | protein | 10 | 0% helix, 0% strand | P00766 |
| B | Gamma-chymotrypsin (EC 3.4.21.1) | protein | 131 | 2% helix, 40% strand | P00766 |
| C | Gamma-chymotrypsin (EC 3.4.21.1) | protein | 97 | 25% helix, 40% strand | P00766 |
| D | Peptide swpw | protein | 4 | 0% helix, 50% strand | — |
| E | Peptide tpgvy | protein | 5 | 0% helix, 60% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
8 interfaces between chains.
- B–C · 2944 Ų buried · 46 hydrogen bonds · protein-protein
- A–B · 480 Ų buried · 2 hydrogen bonds · protein-protein
- C–E · 388 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 374 Ų buried · 8 hydrogen bonds · protein-protein
- D–E · 300 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 5R4B · Crystal Structure of deuterated gamma-Chymotrypsin at pH 9, cryo temperature · the same entry in another collection · chain E against E, TM-score 1.00
- P00766 · AlphaFold monomer V2.0 prediction for chymotrypsinogen a (P00766) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P00766
- Elsewhere: RCSB PDB 5R4B · PDBe 5R4B · UniProt P00766
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