MolNFT v1 · #4771 · protein

Murine collagen ALPHA1(XV), endostatin domain

1DY2 · Collagen ALPHA1(XV) chain: “Murine collagen ALPHA1(XV), endostatin domain”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.35). MolNFT v1 #4771 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1DY2
Type: protein
Length: 168 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Collagen ALPHA1(XV) chain
UniProt: O35206
Ligands: SO4
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Collagen ALPHA1(XV) chain	protein	168	17% helix, 27% strand	O35206

Ligands and binding sites

SO4 · Sulfate ion · ion · 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	72	0.35	0.77	16	SO4

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1DY2 · Murine collagen alpha1(XV), endostatin domain · the same entry in another collection · chain A against A, TM-score 1.00
O35206 · AlphaFold monomer V2.0 prediction for collagen alpha-1(XV) chain (O35206) · a predicted model of the same protein · 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 O35206
Elsewhere: RCSB PDB 1DY2 · PDBe 1DY2 · UniProt O35206

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