MolNFT v1 · #91347 · protein

Specificity and structure of a high affinity activin-like 1 (ALK1) signaling complex

4FAO · GROWTH/DIFFERENTIATION factor 2: “Specificity and structure of a high affinity activin-like 1 (ALK1) signaling complex”. X-ray diffraction, 2 ligands (NAG, NA), 20 pockets (best druggability 0.79). MolNFT v1 #91347 on GenesisL1: 3D…

PDB: 4FAO
Type: protein
Length: 3,233 residues
Chains: 36
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GROWTH/DIFFERENTIATION factor 2; SERINE/THREONINE-protein kinase receptor R3; Activin…
UniProt: Q9UK05, P37023, Q13705
Ligands: NAG, NA
Pockets: 20 · best druggability 0.79

Structure

x-ray diffraction · 5 distinct chains · 11% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, G, H, M, S, T, a, b, g, h	GROWTH/DIFFERENTIATION factor 2	protein	105	14% helix, 50% strand	Q9UK05
C, I, O, U, c, i	SERINE/THREONINE-protein kinase receptor R3	protein	75	7% helix, 35% strand	P37023
D, J, P, V, d, j	SERINE/THREONINE-protein kinase receptor R3	protein	72	7% helix, 36% strand	P37023
E, F, K, L, Q, R, W, X, e, f, k, l	Activin receptor type-2B	protein	91	8% helix, 48% strand	Q13705
N	GROWTH/DIFFERENTIATION factor 2	protein	104	18% helix, 48% strand	Q9UK05

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 24 copies · chains E, F, K, L, Q, R, W, l, X, k, e, f
NA · Sodium ion · metal · 6 copies · chains F, G, K, R, T, X, a, e, k

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	734	0.79	0.83	73	empty
2	795	0.73	0.79	71	empty
3	810	0.73	0.78	66	empty
4	476	0.72	0.82	49	empty
5	195	0.72	0.89	32	empty

Interfaces

69 interfaces between chains.

g–h · 1305 Å² buried · 7 hydrogen bonds · protein-protein
a–b · 1304 Å² buried · 7 hydrogen bonds · protein-protein
S–T · 1300 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 1299 Å² buried · 7 hydrogen bonds · protein-protein
M–N · 1299 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 162 disulfide, 24 glycan (disulfide, N-glycosylation).

Compared structures

4FAO · Specificity and Structure of a high affinity Activin-like 1 (ALK1) signaling complex · the same entry in another collection · chain K against K, 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 Q9UK05
Every structure of UniProt P37023
Every structure of UniProt Q13705
Elsewhere: RCSB PDB 4FAO · PDBe 4FAO · UniProt Q9UK05 · UniProt P37023 · UniProt Q13705

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