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Structure of C34N126K/N36

Analyse Structure of C34N126K/N36 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KTS
Type: protein
Length: 210 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope glycoprotein; Glycoprotein 41
UniProt: C7F2J9, Q6TAN7
Ligands: ACE

Structure

x-ray diffraction · 2 distinct chains · 94% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
N, B, E	Envelope glycoprotein	protein	36	94% helix, 0% strand	C7F2J9
C, A, D	Glycoprotein 41	protein	34	94% helix, 0% strand	Q6TAN7

Ligands and binding sites

ACE · Acetyl group · ligand · 6 copies · chains N, D, C, B, A, E

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

Interfaces

9 interfaces between chains.

N–C · 765 Å² buried · 7 hydrogen bonds · protein-protein
E–D · 762 Å² buried · 4 hydrogen bonds · protein-protein
B–A · 759 Å² buried · 4 hydrogen bonds · protein-protein
N–B · 698 Å² buried · 4 hydrogen bonds · protein-protein
N–E · 694 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

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

Compared structures

6KTS · Structure of C34N126K/N36 · the same entry in another collection · chain N against N, 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 C7F2J9
Every structure of UniProt Q6TAN7
Elsewhere: RCSB PDB 6KTS · PDBe 6KTS · UniProt C7F2J9 · UniProt Q6TAN7

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