MolNFT v1 · #173930 · protein

A double-histidine mutant of HSP47 slows down client release at low pH

7BFI · Collagen-binding protein: “A double-histidine mutant of HSP47 slows down client release at low pH”. X-ray diffraction, 1 ligand (ACE), 20 pockets (best druggability 0.76). MolNFT v1 #173930 on GenesisL1: 3D structure, binding sites…

PDB: 7BFI
Type: protein
Length: 1,567 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Collagen-binding protein; 15R8 collagen model peptide
UniProt: E2RHY7
Ligands: ACE
Pockets: 20 · best druggability 0.76

Structure

x-ray diffraction · 6 distinct chains · 32% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Collagen-binding protein	protein	372	33% helix, 34% strand	E2RHY7
F, H, I, J, E	15R8 collagen model peptide	protein	14	0% helix, 0% strand	—
C	Collagen-binding protein	protein	376	33% helix, 33% strand	E2RHY7
D	Collagen-binding protein	protein	367	33% helix, 34% strand	E2RHY7
B	Collagen-binding protein	protein	369	33% helix, 34% strand	E2RHY7
G	15R8 collagen model peptide	protein	13	0% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 6 copies · chains F, E, G, H, I, J

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

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	885	0.76	0.79	81	empty
2	682	0.76	0.82	56	empty
3	716	0.70	0.77	67	empty
4	810	0.70	0.76	79	empty
5	544	0.65	0.77	63	empty

Interfaces

23 interfaces between chains.

D–B · 746 Å² buried · 16 hydrogen bonds · protein-protein
A–C · 504 Å² buried · 5 hydrogen bonds · protein-protein
I–J · 456 Å² buried · 6 hydrogen bonds · protein-protein
F–G · 452 Å² buried · 5 hydrogen bonds · protein-protein
F–E · 450 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 covalent (covalent ligand).

Compared structures

7BFI · A double-histidine mutant of HSP47 slows down client release at low pH · the same entry in another collection · 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 E2RHY7
Elsewhere: RCSB PDB 7BFI · PDBe 7BFI · UniProt E2RHY7

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