6THB: Attachment glycoprotein

Receptor binding domain of the Cedar Virus attachment glycoprotein (G). Determined by X-ray diffraction at 2.78 Å resolution. Released 18 Dec 2019.

Method: X-ray diffraction
Resolution: 2.78 Å
Organism: Cedar virus
Chains: 2
Atoms: 6,889
Mol. weight: 100.52 kDa
Ligands: NAG
Released: 18 Dec 2019

Explore 6THB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6THB contains 18 α-helices and 68 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 34 β-strands

Element	Residues	Length	Sheet
β-strand	224-226	3	1
β-strand	238-248	11	2
β-strand	251-260	10	2
β-strand	270-280	11	2
β-strand	286-295	10	2
α-helix	299-301	3
β-strand	302-310	9	3
β-strand	313-320	8	3
α-helix	326-329	4
α-helix	332-334	3
β-strand	336-342	7	3
α-helix	347-348	2
β-strand	349-352	4	3
α-helix	355-357	3
β-strand	358-360	3	4
β-strand	366-369	4	4
β-strand	371	1	5
β-strand	375-377	3	4
β-strand	380-389	10	4
α-helix	397-400	4
α-helix	405-407	3
α-helix	412-418	7
β-strand	421	1	4
β-strand	429-438	10	4
β-strand	446-451	6	4
β-strand	452	1	6
α-helix	453	1
β-strand	463-468	6	5
β-strand	471-476	6	5
β-strand	486-492	7	5
β-strand	496	1	6
β-strand	497-500	4	5
β-strand	529-530	2	1
β-strand	533-536	4	7
β-strand	541-547	7	7
β-strand	554	1	8
β-strand	556-561	6	7
β-strand	566-571	6	7
β-strand	578	1	8
β-strand	579-589	11	1
β-strand	592-601	10	1
β-strand	609	1	2
β-strand	612-617	6	1

Chain B: 9 helices, 34 β-strands

Element	Residues	Length	Sheet
β-strand	224-226	3	9
β-strand	238-248	11	10
β-strand	251-260	10	10
β-strand	270-280	11	10
β-strand	286-295	10	10
α-helix	299-301	3
β-strand	302-310	9	11
β-strand	313-320	8	11
α-helix	326-329	4
α-helix	332-334	3
β-strand	336-342	7	11
α-helix	347-348	2
β-strand	349-352	4	11
α-helix	355-357	3
β-strand	359-360	2	12
β-strand	366-368	3	12
β-strand	371	1	13
β-strand	375-377	3	12
β-strand	380-389	10	12
α-helix	399-401	3
α-helix	405-407	3
α-helix	412-419	8
β-strand	421	1	12
β-strand	429-438	10	12
β-strand	446-451	6	12
β-strand	452	1	14
α-helix	453	1
β-strand	463-468	6	13
β-strand	471-476	6	13
β-strand	486-492	7	13
β-strand	496	1	14
β-strand	497-500	4	13
β-strand	529-530	2	9
β-strand	533-536	4	15
β-strand	541-547	7	15
β-strand	554	1	16
β-strand	556-561	6	15
β-strand	566-571	6	15
β-strand	578	1	16
β-strand	579-589	11	9
β-strand	592-601	10	9
β-strand	609	1	10
β-strand	612-617	6	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Attachment glycoprotein	A, B	protein	426	Cedar virus	J7H333 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6THB_1 Attachment glycoprotein (chains A, B)
ETGKIFCKSVSKDPDFRLKQIDYVIPVQQDRSICMNNPLLDISDGFFTYIHYEGINSCKK
SDSFKVLLSHGEIVDRGDYRPSLYLLSSHYHPYSMQVINCVPVTCNQSSFVFCHISNNTK
TLDNSDYSSDEYYITYFNGIDRPKTKKIPINNMTADNRYIHFTFSGGGGVCLGEEFIIPV
TTVINTDVFTHDYCESFNCSVQTGKSLKEICSESLRSPTNSSRYNLNGIMIISQNNMTDF
KIQLNGITYNKLSFGSPGRLSKTLGQVLYYQSSMSWDTYLKAGFVEKWKPFTPNWMNNTV
ISRPNQGNCPRYHKCPEICYGGTYNDIAPLDLGKDMYVSVILDSDQLAENPEITVFNSTT
ILYKERVSKDELNTRSTTTSCFLFLDEPWCISVLETNRFNGKSIRPEIYSYKIPKYCGTK
HHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	13

Primary citation

A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus. Pryce, R., Azarm, K., Rissanen, I. et al. Life Sci Alliance (2020) 3. DOI 10.26508/lsa.201900578 · PubMed

Other PDB entries of the same protein (UniProt J7H333 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6P7Y 2.84 Å, Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein globular domain in…
6P72 3.28 Å, Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein global domain
6P7S 3.49 Å, Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein globular domain in…
6THG 4.07 Å, Cedar Virus attachment glycoprotein (G) in complex with human ephrin-B1

Browse structure collections

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