Research workbench
X-ray structure of the dimeric CCL2 lectin in native form
Analyse X-ray structure of the dimeric CCL2 lectin in native form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4USP
- Type
- protein
- Length
- 270 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CCL2 lectin
- UniProt
- B3GA02
- Ligands
- CL, PO4
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | CCL2 lectin | protein | 135 | 2% helix, 47% strand | B3GA02 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 683 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4USP · X-ray structure of the dimeric CCL2 lectin in native form · 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 B3GA02
- Elsewhere: RCSB PDB 4USP · PDBe 4USP · UniProt B3GA02
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