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Hrsv M2-1 mutant S58D S61D, P21 crystal

Analyse Hrsv M2-1 mutant S58D S61D, P21 crystal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4C3E
Type: protein
Length: 2,639 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Matrix M2-1
UniProt: P04545
Ligands: ZN
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 13 distinct chains · 70% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Matrix M2-1	protein	172	67% helix, 1% strand	P04545
B	Matrix M2-1	protein	168	69% helix, 1% strand	P04545
C	Matrix M2-1	protein	171	68% helix, 1% strand	P04545
D	Matrix M2-1	protein	167	70% helix, 1% strand	P04545
E, F, P	Matrix M2-1	protein	160	70% helix, 1% strand	P04545
G	Matrix M2-1	protein	167	69% helix, 1% strand	P04545
H, L	Matrix M2-1	protein	163	71% helix, 1% strand	P04545
I	Matrix M2-1	protein	164	71% helix, 1% strand	P04545
J	Matrix M2-1	protein	166	70% helix, 1% strand	P04545
K	Matrix M2-1	protein	165	70% helix, 1% strand	P04545
M	Matrix M2-1	protein	155	72% helix, 1% strand	P04545
N	Matrix M2-1	protein	170	68% helix, 1% strand	P04545
O	Matrix M2-1	protein	168	69% helix, 1% strand	P04545

Ligands and binding sites

ZN · Zinc ion · metal · 16 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P

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	1141	0.86	0.87	107	empty
2	669	0.83	0.87	66	empty
3	601	0.83	0.88	75	empty
4	629	0.83	0.87	63	empty
5	538	0.81	0.87	57	empty

Interfaces

45 interfaces between chains.

A–C · 1792 Å² buried · 24 hydrogen bonds · protein-protein
B–I · 1784 Å² buried · 24 hydrogen bonds · protein-protein
D–J · 1780 Å² buried · 25 hydrogen bonds · protein-protein
A–F · 1764 Å² buried · 21 hydrogen bonds · protein-protein
D–K · 1760 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

4C3E · HRSV M2-1 mutant S58D S61D, P21 crystal · the same entry in another collection · chain B against B, 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 P04545
Elsewhere: RCSB PDB 4C3E · PDBe 4C3E · UniProt P04545

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