5CFA: Bone sialoprotein-binding protein

Crystal structures of Bbp from Staphylococcus aureus with peptide ligand. Determined by X-ray diffraction at 1.45 Å resolution. Released 23 Sept 2015.

Method: X-ray diffraction
Resolution: 1.45 Å
Organisms: Staphylococcus aureus, Homo sapiens
Chains: 4
Atoms: 6,310
Mol. weight: 76.36 kDa
Ligands: MG
Released: 23 Sept 2015

Explore 5CFA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5CFA contains 13 α-helices and 58 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: 6 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	1
α-helix	6-8	3
β-strand	9-18	10	1
β-strand	25-27	3	1
α-helix	28-30	3
β-strand	34-42	9	1
β-strand	51-55	5	1
β-strand	60-61	2	2
α-helix	71-73	3
β-strand	74-75	2	1
β-strand	81-88	8	1
β-strand	93-98	6	1
α-helix	101-104	4
β-strand	105-116	12	1
β-strand	117-118	2	2
β-strand	127-135	9	1
β-strand	138-147	10	1
β-strand	152-154	3	3
β-strand	157-167	11	3
β-strand	172-179	8	3
β-strand	186-195	10	4
β-strand	197-198	2	5
β-strand	204-205	2	5
β-strand	212	1	3
β-strand	218-223	6	3
β-strand	243-244	2	3
α-helix	246-248	3
β-strand	250-256	7	4
β-strand	259-267	9	4
β-strand	271-278	8	3
α-helix	283-286	4
β-strand	291-298	8	4
β-strand	304-316	13	4
β-strand	319-326	8	1

Chain B: 7 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	6
α-helix	6-8	3
β-strand	9-18	10	6
β-strand	25-27	3	6
α-helix	28-30	3
β-strand	34-42	9	6
β-strand	51-55	5	6
β-strand	60-61	2	7
α-helix	71-73	3
β-strand	74-75	2	6
β-strand	81-88	8	6
β-strand	93-98	6	6
α-helix	101-104	4
β-strand	105-116	12	6
β-strand	117-118	2	7
β-strand	127-135	9	6
β-strand	138-147	10	6
β-strand	152-154	3	8
β-strand	157-167	11	8
β-strand	172-179	8	8
β-strand	186-195	10	9
β-strand	197-198	2	10
β-strand	204-205	2	10
β-strand	212	1	8
β-strand	218-223	6	8
α-helix	224-225	2
β-strand	243-244	2	8
α-helix	246-248	3
β-strand	250-256	7	9
β-strand	259-267	9	9
β-strand	271-278	8	8
α-helix	283-286	4
β-strand	290-298	9	9
β-strand	304-316	13	9
β-strand	319-326	8	6

Chains C and D: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	28-33	6	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bone sialoprotein-binding protein	A, B	protein	331	Staphylococcus aureus	Q14U76 (AlphaFold model)
Peptide from Fibrinogen alpha chain	C, D	protein	15	Homo sapiens	P02671 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5CFA_1 Bone sialoprotein-binding protein (chains A, B)
GPLGSNNVNDLITVTKQMITEGIKDDGVIQAHDGEHIIYTSDFKIDNAVKAGDTMTVKYD
KHTIPSDITDDFTPVDITDPSGEVIAKGTFDLNTKTITYKFTDYVDRYENVNAKLELNSY
IDKKEVPNETNLNLTFATADKETSKNVKVEYQKPIVKDESNIQSIFSHLDTTKHEVEQTI
YVNPLKLNAKNTNVTIKSGGVADNGDYYTGDGSTIIDSNTEIKVYKVASGQQLPQSNKIY
DYSQYEDVTNSVTINKNYGTNMANINFGDIDSAYIVKVVSKYTPGAEDDLAVQQGVRMTT
TNKYNYSSYAGYTNTILSTTDSGGGDGTVKP

Sequence of entity 2 (C, D), FASTA

>5CFA_2 Peptide from Fibrinogen alpha chain (chains C, D)
SKQFTSSTSYNRGDS

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1

Primary citation

Crystal structures of Bbp from Staphylococcus aureus reveal the ligand binding mechanism with Fibrinogen alpha. Zhang, X.Y., Wu, M., Zhuo, W. et al. Protein Cell (2015) 6:757-766. DOI 10.1007/s13238-015-0205-x · PubMed

Other PDB entries of the same protein (UniProt Q14U76 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5CF3 2.03 Å, Crystal structures of Bbp from Staphylococcus aureus

Browse structure collections

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