4AVT: CPHPC

Structure of CPHPC bound to Serum Amyloid P Component. Determined by X-ray diffraction at 3.2 Å resolution. Released 19 Jun 2013.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: HOMO SAPIENS
Chains: 10
Atoms: 16,782
Mol. weight: 237.54 kDa
Ligands: NAG, GHE, CA
Released: 19 Jun 2013

Explore 4AVT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4AVT contains 41 α-helices and 220 β-strands across 10 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.

Chains A, B, D and G: 4 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	1
β-strand	7-11	5	2
β-strand	19-22	4	3
α-helix	29	1
β-strand	30	1	4
β-strand	32-40	9	2
β-strand	47-54	8	3
β-strand	57-67	11	3
β-strand	70-75	6	3
β-strand	78-83	6	3
β-strand	92-99	8	2
β-strand	104-107	4	2
β-strand	108-109	2	5
β-strand	112-113	2	5
β-strand	117-118	2	2
β-strand	125	1	4
β-strand	130-133	4	3
α-helix	146-148	3
β-strand	152-160	9	2
α-helix	166-173	8
α-helix	177-180	4
β-strand	183-184	2	2
β-strand	187	1	2
β-strand	188	1	1
β-strand	190-193	4	3
β-strand	197-200	4	2

Chains C, E, H and J: 4 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	11
β-strand	7-11	5	12
β-strand	19-22	4	13
α-helix	29	1
β-strand	30	1	14
β-strand	32-40	9	12
β-strand	47-54	8	13
β-strand	57-67	11	13
β-strand	70-75	6	13
β-strand	78-83	6	13
β-strand	92-99	8	12
β-strand	104-107	4	12
β-strand	108-109	2	15
β-strand	112-113	2	15
β-strand	117-118	2	12
β-strand	125	1	14
β-strand	130-133	4	13
α-helix	146-148	3
β-strand	152-160	9	12
α-helix	166-173	8
α-helix	177-179	3
β-strand	183-184	2	12
β-strand	187	1	12
β-strand	188	1	11
β-strand	190-193	4	13
β-strand	197-200	4	12

Chain F: 4 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	26
β-strand	7-11	5	27
β-strand	19-22	4	28
α-helix	29	1
β-strand	30	1	29
β-strand	32-40	9	27
β-strand	47-54	8	28
β-strand	57-67	11	28
β-strand	70-75	6	28
β-strand	78-83	6	28
β-strand	91-99	9	27
β-strand	104-107	4	27
β-strand	108-109	2	30
β-strand	112-113	2	30
β-strand	117-118	2	27
β-strand	125	1	29
β-strand	130-133	4	28
α-helix	146-148	3
β-strand	152-160	9	27
α-helix	166-173	8
α-helix	177-179	3
β-strand	183-184	2	27
β-strand	187	1	27
β-strand	188	1	26
β-strand	190-193	4	28
β-strand	197-200	4	27

Chain I: 5 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	41
β-strand	7-11	5	42
β-strand	19-22	4	43
α-helix	29	1
β-strand	30	1	44
β-strand	32-40	9	42
β-strand	47-54	8	43
β-strand	57-67	11	43
β-strand	70-75	6	43
β-strand	78-83	6	43
β-strand	92-99	8	42
β-strand	104-107	4	42
β-strand	108-109	2	45
β-strand	112-113	2	45
β-strand	117-118	2	42
β-strand	125	1	44
β-strand	130-133	4	43
α-helix	146-148	3
β-strand	152-160	9	42
α-helix	163-165	3
α-helix	166-173	8
α-helix	177-179	3
β-strand	183-184	2	42
β-strand	187	1	42
β-strand	188	1	41
β-strand	190-193	4	43
β-strand	197-200	4	42

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serum amyloid P-component	A, B, C, D, E, F, G, H, I, J	protein	204	HOMO SAPIENS	P02743 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J), FASTA

>4AVT_1 SERUM AMYLOID P-COMPONENT (chains A, B, C, D, E, F, G, H, I, J)
HTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNE
LLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLR
QGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPA
NILDWQALNYEIRGYVIIKPLVWV

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	10
GHE	(2R)-1-[6-[(2R)-2-carboxypyrrolidin-1-yl]-6-oxidanylidene-hexanoyl]pyrrolidine-…	C16 H24 N2 O6	5
CA	Calcium ion	Ca	20

Primary citation

Interaction of Serum Amyloid P Component with Hexanoyl Bis(D-Proline) (Cphpc). Kolstoe, S.E., Jenvey, M.C., Purvis, A. et al. Acta Crystallogr D Biol Crystallogr (2014) 70:2232. DOI 10.1107/S1399004714013455 · PubMed

Other PDB entries of the same protein (UniProt P02743 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4AVS 1.4 Å, Structure of N-Acetyl-L-Proline bound to Serum Amyloid P Component
3KQR 1.5 Å, The structure of serum amyloid p component bound to phosphoethanolamine
4AYU 1.5 Å, Structure of N-Acetyl-D-Proline bound to serum amyloid P component
4AVV 1.6 Å, Structure of CPHPC bound to Serum Amyloid P Component
2W08 1.7 Å, The structure of serum amyloid P component bound to 0-phospho- threonine
1SAC 2.0 Å, The structure of pentameric human serum amyloid P component
2A3Y 2.0 Å, Pentameric crystal structure of human serum amyloid P-component bound to…
1GYK 2.2 Å, Serum Amyloid P Component co-crystallised with MOBDG at neutral pH
2A3W 2.2 Å, Decameric structure of human serum amyloid P-component bound to…
1LGN 2.8 Å, Decameric damp complex of human serum amyloid P component
3D5O 2.8 Å, Structural recognition and functional activation of FcrR by innate pentraxins
2A3X 3.0 Å, Decameric crystal structure of human serum amyloid P-component bound to…

Browse structure collections

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