Research workbench
X-ray analyses of aspartic PROTEINASES.III. three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin at 1.6 ångströms resolution
Analyse X-ray analyses of aspartic PROTEINASES.III. three-dimensional structure of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ER7
- Type
- protein
- Length
- 337 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11838
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | — | protein | 330 | — | P11838 |
| I | — | protein | 7 | — | — |
Compared structures
- 2ER7 · X-ray analyses of aspartic PROTEINASES.III. three-dimensional structure of endothiapepsin… · the same entry in another collection · chain E against E, TM-score 1.00
- P11838 · AlphaFold monomer V2.0 prediction for endothiapepsin (P11838) · 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 P11838
- Elsewhere: RCSB PDB 2ER7 · PDBe 2ER7 · UniProt P11838
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