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Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ibeta
Analyse Crystal structure of the C-terminal peptidoglycan-binding domain of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EAV
- Type
- protein
- Length
- 328 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidoglycan recognition protein-I-beta
- UniProt
- Q3B822
- Ligands
- NI
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Peptidoglycan recognition protein-I-beta | protein | 164 | 31% helix, 21% strand | Q3B822 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 734 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 2EAV · Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan… · 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 Q3B822
- Elsewhere: RCSB PDB 2EAV · PDBe 2EAV · UniProt Q3B822
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