MolNFT v1 · #191534 · protein
Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis
8TLN: “Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion…”. X-ray diffraction, 2 ligands (CA, ZN). MolNFT v1 #191534 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 8TLN
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00800
- Ligands
- CA, ZN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | — | protein | 318 | — | P00800 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains E
- ZN · Zinc ion · metal · chains E
- DMS · Dimethyl sulfoxide · additive · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 8TLN · Structural comparison suggests that thermolysin and related neutral proteases undergo… · the same entry in another collection · chain E against E, TM-score 1.00
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 P00800
- Elsewhere: RCSB PDB 8TLN · PDBe 8TLN · UniProt P00800
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