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Crystal structure of human alpha-defensin-6

Analyse Crystal structure of human alpha-defensin-6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZMQ
Type: protein
Length: 128 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Defensin 6
UniProt: Q01524
Ligands: CL

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 66% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Defensin 6	protein	32	0% helix, 66% strand	Q01524

Ligands and binding sites

CL · Chloride ion · ion · 8 copies · chains A, C, D, B

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

Interfaces

5 interfaces between chains.

A–C · 438 Å² buried · 7 hydrogen bonds · protein-protein
A–D · 402 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 389 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 299 Å² buried · 4 hydrogen bonds · protein-protein
C–D · 285 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

1ZMQ · Crystal structure of human alpha-defensin-6 · the same entry in another collection · chain D against D, TM-score 1.00
Q01524 · AlphaFold monomer V2.0 prediction for defensin-6 (Q01524) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 Q01524
Elsewhere: RCSB PDB 1ZMQ · PDBe 1ZMQ · UniProt Q01524

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