Research workbench

Structure of a novel hyaluronidase (HYAL_SK) from streptomyces koganeiensis.

Analyse Structure of a novel hyaluronidase (HYAL_SK) from streptomyces koganeiensis. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UFQ
Type: protein
Length: 423 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hyaluronidase
UniProt: A0A0U2E2J7
Ligands: NA, SO4, CL

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hyaluronidase	protein	212	0% helix, 15% strand	A0A0U2E2J7
B	Hyaluronidase	protein	211	0% helix, 16% strand	A0A0U2E2J7

Ligands and binding sites

NA · Sodium ion · metal · 5 copies · chains A, B
SO4 · Sulfate ion · ion · 5 copies · chains A, B
CL · Chloride ion · ion · chains A
PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains A
GOL · Glycerol · additive · 2 copies · chains B

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

Interfaces

1 interface between chains.

A–B · 40 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

4UFQ · Structure of a novel Hyaluronidase (Hyal_Sk) from Streptomyces koganeiensis. · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A0U2E2J7
Elsewhere: RCSB PDB 4UFQ · PDBe 4UFQ · UniProt A0A0U2E2J7

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.