2VR3: Clumping factor A

Structural and Biochemical Characterization of Fibrinogen binding to ClfA from Staphylocccus aureus. Determined by X-ray diffraction at 1.95 Å resolution. Released 19 May 2009.

Method: X-ray diffraction
Resolution: 1.95 Å
Organisms: STAPHYLOCOCCUS AUREUS, HOMO SAPIENS
Chains: 4
Atoms: 5,226
Mol. weight: 74.16 kDa
Released: 19 May 2009

Explore 2VR3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2VR3 contains 15 α-helices and 62 β-strands across 4 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: 7 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	231	1	1
α-helix	233-235	3
β-strand	237-244	8	1
β-strand	248-249	2	1
β-strand	253	1	2
β-strand	257-265	9	1
α-helix	266	1
β-strand	274-278	5	1
β-strand	283-284	2	3
β-strand	287	1	2
β-strand	289	1	4
α-helix	294-296	3
β-strand	297-298	2	1
β-strand	305-309	5	1
β-strand	315-319	5	1
α-helix	322-325	4
β-strand	326-337	12	1
β-strand	338-339	2	3
β-strand	348-356	9	1
β-strand	359-367	9	1
β-strand	373-375	3	5
β-strand	378-388	11	5
β-strand	393-400	8	5
β-strand	407-416	10	2
α-helix	417	1
β-strand	424-425	2	5
β-strand	432-437	6	5
α-helix	441-443	3
β-strand	457	1	5
α-helix	459-461	3
β-strand	463-468	6	2
β-strand	471-475	5	2
β-strand	482-483	2	2
β-strand	487-495	9	5
β-strand	505-512	8	2
β-strand	518-530	13	2
β-strand	533-540	8	1

Chain B: 8 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	231	1	6
α-helix	233-235	3
β-strand	237-244	8	6
β-strand	248-249	2	6
β-strand	253	1	7
β-strand	257-265	9	6
α-helix	266	1
β-strand	274-278	5	6
β-strand	283-284	2	8
β-strand	287	1	7
β-strand	289	1	9
α-helix	293-296	4
β-strand	297-299	3	6
β-strand	302-309	8	6
β-strand	315-319	5	6
α-helix	321-324	4
β-strand	326-337	12	6
β-strand	338-339	2	8
β-strand	348-356	9	6
β-strand	359-367	9	6
β-strand	373-375	3	9
β-strand	378-388	11	9
β-strand	393-400	8	9
β-strand	407-416	10	7
α-helix	417	1
β-strand	424-425	2	9
β-strand	432-437	6	9
α-helix	441-443	3
α-helix	452-454	3
β-strand	456-457	2	9
α-helix	459-461	3
β-strand	463-468	6	7
β-strand	471-475	5	7
β-strand	482-483	2	7
β-strand	487-495	9	9
β-strand	504-512	9	7
β-strand	518-530	13	7
β-strand	533-540	8	6

Chain C: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	401-410	10	2

Chain D: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	400-410	11	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Clumping factor A	A, B	protein	329	STAPHYLOCOCCUS AUREUS	Q2G015 (AlphaFold model)
Fibrinogen gamma-chain	C, D	protein	13	HOMO SAPIENS	P02679 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2VR3_1 CLUMPING FACTOR A (chains A, B)
MRGSHHHHHHGSGTDITNQLTNVTVGIDSGTTVYPHQAGYVKLNYGFSVPNSAVKGDTFK
ITVPKELNLNGVTSTAKVPPIMAGDQVLANGVIDSDGNVIYTFTDYVNTKCDVKATLTMP
AYIDPENVKKTGNVTLATGIGSTTANKTVLVDYEKYGKFYNLSIKGTIDQIDKTNNTYRQ
TIYVNPSGDNVIAPVLTGNLKPNTDSNALIDQQNTSIKVYKVDNAADLSESYFVNPENFE
DVTNSVNITFPNPNQYKVEFNTPDDQITTPYIVVVNGHIDPNSKGDLALRSTLYGYNSNI
IWRSMSWDNEVAFNNGSGSGDGIDCPVVP

Sequence of entity 2 (C, D), FASTA

>2VR3_2 FIBRINOGEN GAMMA-CHAIN (chains C, D)
QHHLGGAKQAGAV

Primary citation

A Structural Model of the Staphylococcus Aureus Clfa-Fibrinogen Interaction Opens New Avenues for the Design of Anti-Staphylococcal Therapeutics. Ganesh, V.K., Rivera, J.J., Smeds, E. et al. PLoS Pathog (2008) 4:226. DOI 10.1371/JOURNAL.PPAT.1000226 · PubMed

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