4AVS: N-Acetyl-L-Proline

Structure of N-Acetyl-L-Proline bound to Serum Amyloid P Component. Determined by X-ray diffraction at 1.4 Å resolution. Released 19 Jun 2013.

Method: X-ray diffraction
Resolution: 1.4 Å
Organism: HOMO SAPIENS
Chains: 5
Atoms: 9,823
Mol. weight: 118.7 kDa
Ligands: N7P, CA, NAG
Released: 19 Jun 2013

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

Secondary structure: helices and β-sheets

4AVS contains 24 α-helices and 100 β-strands across 5 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: 5 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	1
β-strand	7-11	5	2
β-strand	19-22	4	3
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	104-109	6	2
β-strand	112-113	2	2
α-helix	114-116	3
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	163-165	3
α-helix	166-174	9
α-helix	177-179	3
β-strand	183-184	2	2
β-strand	188	1	1
β-strand	190-193	4	3
β-strand	197-200	4	2

Chain B: 6 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	5
β-strand	7-11	5	6
β-strand	19-22	4	7
β-strand	30	1	8
β-strand	32-40	9	6
β-strand	47-54	8	7
β-strand	57-67	11	7
β-strand	70-75	6	7
β-strand	78-83	6	7
β-strand	92-99	8	6
β-strand	104-109	6	6
β-strand	112-113	2	6
α-helix	114-116	3
β-strand	117-118	2	6
β-strand	125	1	8
α-helix	126	1
β-strand	130-133	4	7
α-helix	146-148	3
β-strand	152-160	9	6
α-helix	166-173	8
α-helix	177-179	3
β-strand	183-184	2	6
α-helix	185-187	3
β-strand	188	1	5
β-strand	190-193	4	7
β-strand	197-200	4	6

Chain C: 4 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	9
β-strand	7-11	5	10
β-strand	19-22	4	11
β-strand	30	1	12
β-strand	32-40	9	10
β-strand	47-54	8	11
β-strand	57-67	11	11
β-strand	70-75	6	11
β-strand	78-83	6	11
β-strand	92-99	8	10
β-strand	104-109	6	10
β-strand	112-113	2	10
α-helix	114-116	3
β-strand	117-118	2	10
β-strand	125	1	12
β-strand	130-133	4	11
α-helix	146-148	3
β-strand	152-160	9	10
α-helix	166-173	8
α-helix	177-179	3
β-strand	183-184	2	10
β-strand	188	1	9
β-strand	190-193	4	11
β-strand	197-200	4	10

Chain D: 5 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	13
β-strand	7-11	5	14
β-strand	19-22	4	15
β-strand	30	1	16
β-strand	32-40	9	14
β-strand	47-54	8	15
β-strand	57-67	11	15
β-strand	70-75	6	15
β-strand	78-83	6	15
β-strand	92-99	8	14
β-strand	104-109	6	14
β-strand	112-113	2	14
α-helix	114-116	3
β-strand	117-118	2	14
β-strand	125	1	16
β-strand	130-133	4	15
α-helix	146-148	3
β-strand	152-160	9	14
α-helix	166-173	8
α-helix	177-179	3
β-strand	183-184	2	14
α-helix	185-187	3
β-strand	188	1	13
β-strand	190-193	4	15
β-strand	197-200	4	14

Chain E: 4 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	17
β-strand	7-11	5	18
β-strand	19-22	4	19
β-strand	30	1	20
β-strand	32-40	9	18
β-strand	47-54	8	19
β-strand	57-67	11	19
β-strand	70-75	6	19
β-strand	78-83	6	19
β-strand	92-99	8	18
β-strand	104-109	6	18
β-strand	112-113	2	18
α-helix	114-116	3
β-strand	117-118	2	18
β-strand	125	1	20
β-strand	130-133	4	19
α-helix	146-148	3
β-strand	152-160	9	18
α-helix	166-174	9
α-helix	177-179	3
β-strand	183-184	2	18
β-strand	188	1	17
β-strand	190-193	4	19
β-strand	197-200	4	18

Molecules and chains

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

Sequence of entity 1 (A, B, C, D, E), FASTA

>4AVS_1 SERUM AMYLOID P-COMPONENT (chains A, B, C, D, E)
HTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNE
LLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLR
QGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPA
NILDWQALNYEIRGYVIIKPLVWV

Ligands and cofactors

ID	Name	Formula	Copies
N7P	1-acetyl-L-proline	C7 H11 N O3	5
CA	Calcium ion	Ca	10
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	5

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:

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…
4AVT 3.2 Å, Structure of CPHPC bound to Serum Amyloid P Component

Browse structure collections

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