MolNFT v1 · #9270 · protein

Cofilin homology domain of a yeast actin-binding protein ABP1P

1HQZ: “Cofilin homology domain of a yeast actin-binding protein ABP1P”. X-ray diffraction, 15 pockets (best druggability 0.85). MolNFT v1 #9270 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1HQZ
Type: protein
Length: 1,226 residues
Chains: 9
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Actin-binding protein
UniProt: P15891
Pockets: 15 · best druggability 0.85

Structure

x-ray diffraction · 6 distinct chains · 34% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
1, 2	Actin-binding protein	protein	139	35% helix, 23% strand	P15891
3	Actin-binding protein	protein	135	35% helix, 25% strand	P15891
4, 6, 9	Actin-binding protein	protein	137	34% helix, 23% strand	P15891
5	Actin-binding protein	protein	136	33% helix, 25% strand	P15891
7	Actin-binding protein	protein	134	32% helix, 24% strand	P15891
8	Actin-binding protein	protein	132	33% helix, 24% strand	P15891

Pockets

15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1068	0.85	0.85	106	empty
2	697	0.73	0.79	51	empty
3	719	0.70	0.77	54	empty
4	650	0.69	0.77	75	empty
5	539	0.66	0.77	59	empty

Interfaces

17 interfaces between chains.

5–6 · 1027 Å² buried · 11 hydrogen bonds · protein-protein
3–4 · 999 Å² buried · 10 hydrogen bonds · protein-protein
7–8 · 855 Å² buried · 8 hydrogen bonds · protein-protein
1–2 · 608 Å² buried · 2 hydrogen bonds · protein-protein
3–5 · 425 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1HQZ · Cofilin homology domain of a yeast actin-binding protein ABP1P · the same entry in another collection · chain 9 against 9, TM-score 1.00
P15891 · AlphaFold monomer V2.0 prediction for actin-binding protein (P15891) · a predicted model of the same protein · chain 6 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 P15891
Elsewhere: RCSB PDB 1HQZ · PDBe 1HQZ · UniProt P15891

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