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Crystal structure of leucurolysin-a complexed with an endogenous tripeptide (qsw).
Analyse Crystal structure of leucurolysin-a complexed with an endogenous tripeptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Q1L
- Type
- protein
- Length
- 205 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Snake venom metalloproteinase leucurolysin-a; Gln-ser-TRP
- EC
- 3.4.24.-
- UniProt
- P84907
- Ligands
- CA, ZN
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Snake venom metalloproteinase leucurolysin-a (EC 3.4.24.-) | protein | 202 | 41% helix, 18% strand | P84907 |
| D | Gln-ser-TRP | protein | 3 | 0% helix, 0% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- ZN · Zinc ion · metal · chains A, D
- ACT · Acetate ion · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–D · 326 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 4Q1L · Crystal structure of Leucurolysin-a complexed with an endogenous tripeptide (QSW). · the same entry in another collection · chain A against A, TM-score 1.00
- P84907 · AlphaFold monomer V2.0 prediction for snake venom metalloproteinase leucurolysin-a… · a predicted model of the same protein · chain A 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 P84907
- Elsewhere: RCSB PDB 4Q1L · PDBe 4Q1L · UniProt P84907
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