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Crystal structure of human BMP9 at 1.87 a resolution

Analyse Crystal structure of human BMP9 at 1.87 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5I05
Type: protein
Length: 107 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GROWTH/DIFFERENTIATION factor 2
UniProt: Q9UK05

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GROWTH/DIFFERENTIATION factor 2	protein	107	14% helix, 45% strand	Q9UK05

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A

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

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

5I05 · Crystal structure of human BMP9 at 1.87 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
Q9UK05 · AlphaFold monomer V2.0 prediction for GROWTH/DIFFERENTIATION factor 2 (Q9UK05) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 Q9UK05
Elsewhere: RCSB PDB 5I05 · PDBe 5I05 · UniProt Q9UK05

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