MolNFT v1 · #113166 · protein

Kshv lana (ORF73) C-terminal domain, open non-ring conformation: orthorhombic crystal form

5A76 · Orf 73: “Kshv lana (ORF73) C-terminal domain, open non-ring conformation: orthorhombic crystal form”. X-ray diffraction, 1 ligand (MG), 11 pockets (best druggability 0.79). MolNFT v1 #113166 on GenesisL1: 3D structure, binding sites…

PDB: 5A76
Type: protein
Length: 913 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Orf 73
UniProt: Q76SB0
Ligands: MG
Pockets: 11 · best druggability 0.79

Structure

x-ray diffraction · 8 distinct chains · 37% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Orf 73	protein	109	38% helix, 32% strand	Q76SB0
B	Orf 73	protein	113	37% helix, 29% strand	Q76SB0
C	Orf 73	protein	114	36% helix, 31% strand	Q76SB0
D	Orf 73	protein	113	37% helix, 31% strand	Q76SB0
E	Orf 73	protein	116	36% helix, 33% strand	Q76SB0
F	Orf 73	protein	118	36% helix, 31% strand	Q76SB0
G	Orf 73	protein	116	36% helix, 22% strand	Q76SB0
H	Orf 73	protein	114	37% helix, 29% strand	Q76SB0

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains A, C, E, G

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

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1138	0.79	0.81	88	empty
2	687	0.75	0.81	48	empty
3	588	0.74	0.81	52	empty
4	142	0.60	0.84	30	empty
5	102	0.35	0.74	19	MG

Interfaces

14 interfaces between chains.

E–F · 1319 Å² buried · 16 hydrogen bonds · protein-protein
G–H · 1283 Å² buried · 15 hydrogen bonds · protein-protein
C–D · 1250 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 1242 Å² buried · 16 hydrogen bonds · protein-protein
B–E · 450 Å² buried · 3 hydrogen bonds · protein-protein

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 Q76SB0
Elsewhere: RCSB PDB 5A76 · PDBe 5A76 · UniProt Q76SB0

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