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Crystal structure of the cc chemokine CCL14

Analyse Crystal structure of the cc chemokine CCL14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Q8T
Type: protein
Length: 256 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CCL14
UniProt: Q16627
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 3 distinct chains · 19% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CCL14	protein	62	19% helix, 29% strand	Q16627
B, C	CCL14	protein	65	18% helix, 28% strand	Q16627
D	CCL14	protein	64	20% helix, 28% strand	Q16627

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	198	0.66	0.85	39	empty

Interfaces

6 interfaces between chains.

A–B · 839 Å² buried · 10 hydrogen bonds · protein-protein
C–D · 811 Å² buried · 10 hydrogen bonds · protein-protein
B–D · 466 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 382 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 230 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

2Q8T · Crystal Structure of the CC chemokine CCL14 · the same entry in another collection · chain D against D, TM-score 1.00
Q16627 · AlphaFold monomer V2.0 prediction for C-C motif chemokine 14 (Q16627) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 Q16627
Elsewhere: RCSB PDB 2Q8T · PDBe 2Q8T · UniProt Q16627

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