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N-terminal NC4 domain of collagen IX

Analyse N-terminal NC4 domain of collagen IX in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2UUR
Type: protein
Length: 210 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Collagen alpha-1(IX) chain
UniProt: P20849
Ligands: ZN, SO4
Pockets: 1 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Collagen alpha-1(IX) chain	protein	210	13% helix, 43% strand	P20849

Ligands and binding sites

ZN · Zinc ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 5 copies · chains A

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	52	0.41	0.82	16	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2UUR · N-terminal NC4 domain of collagen IX · the same entry in another collection · chain A against A, TM-score 1.00
P20849 · AlphaFold monomer V2.0 prediction for collagen alpha-1(IX) chain (P20849) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P20849
Elsewhere: RCSB PDB 2UUR · PDBe 2UUR · UniProt P20849

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