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Crystal structure of human recombinant interleukin-4 at 2.25 ångströms resolution

Analyse Crystal structure of human recombinant interleukin-4 at 2.25 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RCB
Type: protein
Length: 129 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interleukin-4
UniProt: P05112
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Interleukin-4	protein	129	63% helix, 5% strand	P05112

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	84	0.35	0.75	19	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1RCB · Crystal structure of human recombinant interleukin-4 at 2.25 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
P05112 · AlphaFold monomer V2.0 prediction for interleukin-4 (P05112) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P05112
Elsewhere: RCSB PDB 1RCB · PDBe 1RCB · UniProt P05112

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