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Crystal structure analysis of MIP2

Analyse Crystal structure analysis of MIP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3N52
Type: protein
Length: 275 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-X-C motif chemokine 2
UniProt: P10889
Pockets: 1 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 23% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	C-X-C motif chemokine 2	protein	67	21% helix, 31% strand	P10889
B	C-X-C motif chemokine 2	protein	71	24% helix, 30% strand	P10889
D	C-X-C motif chemokine 2	protein	70	24% helix, 30% strand	P10889

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	965	0.83	0.84	85	empty

Interfaces

6 interfaces between chains.

A–B · 1014 Å² buried · 13 hydrogen bonds · protein-protein
C–D · 967 Å² buried · 12 hydrogen bonds · protein-protein
A–C · 745 Å² buried · 13 hydrogen bonds · protein-protein
B–D · 605 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 132 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

3N52 · crystal Structure analysis of MIP2 · the same entry in another collection · chain D against D, TM-score 1.00
P10889 · AlphaFold monomer V2.0 prediction for C-X-C motif chemokine 2 (P10889) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 P10889
Elsewhere: RCSB PDB 3N52 · PDBe 3N52 · UniProt P10889

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