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Crystal structure of human alpha-defensin-4

Analyse Crystal structure of human alpha-defensin-4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZMM
Type: protein
Length: 128 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neutrophil defensin 4
UniProt: P12838
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 59% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Neutrophil defensin 4	protein	31	0% helix, 61% strand	P12838
B, D	Neutrophil defensin 4	protein	33	0% helix, 58% strand	P12838

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	359	0.57	0.75	35	empty

Interfaces

3 interfaces between chains.

C–D · 344 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 335 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 134 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

1ZMM · Crystal structure of human alpha-defensin-4 · the same entry in another collection · chain D against D, TM-score 1.00
P12838 · AlphaFold monomer V2.0 prediction for neutrophil defensin 4 (P12838) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P12838
Elsewhere: RCSB PDB 1ZMM · PDBe 1ZMM · UniProt P12838

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