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Crystal structure of human adenovirus 2 proteinase with its 11 amino acid cofactor at 1.6 ångström resolution
Analyse Crystal structure of human adenovirus 2 proteinase with its 11 amino acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NLN
- Type
- protein
- Length
- 214 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenain; Pvic
- EC
- 3.4.22.39
- UniProt
- P03252
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenain (EC 3.4.22.39) | protein | 203 | 42% helix, 17% strand | P03252 |
| B | Pvic | protein | 11 | 0% helix, 64% strand | — |
Ligands and binding sites
- ACY · Acetic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 883 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1NLN · Crystal structure of human adenovirus 2 proteinase with its 11 amino acid cofactor at 1.6… · the same entry in another collection · chain A against A, 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 P03252
- Elsewhere: RCSB PDB 1NLN · PDBe 1NLN · UniProt P03252
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