Research workbench

Human beta-defensin-1 (mutant GLN24GLU)

Analyse Human beta-defensin-1 (mutant GLN24GLU) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NLP
Type: protein
Length: 144 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-defensin 1
UniProt: P60022
Ligands: SO4
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Beta-defensin 1	protein	36	17% helix, 33% strand	P60022

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	62	0.39	0.80	16	empty

Interfaces

1 interface between chains.

C–D · 335 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

2NLP · Human beta-defensin-1 (Mutant Gln24Glu) · the same entry in another collection · chain D against D, TM-score 1.00
P60022 · AlphaFold monomer V2.0 prediction for beta-defensin 1 (P60022) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P60022
Elsewhere: RCSB PDB 2NLP · PDBe 2NLP · UniProt P60022

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