1H03: Human CD55 domains 3 & 4

Human CD55 domains 3 & 4. Determined by X-ray diffraction at 1.7 Å resolution. Released 20 Mar 2003.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 2,078
Mol. weight: 27.17 kDa
Released: 20 Mar 2003

Explore 1H03 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1H03 contains 9 α-helices and 38 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 P: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	1
α-helix	7-9	3
β-strand	16-19	4	2
β-strand	25	1	1
β-strand	29-34	6	2
β-strand	38-41	4	3
β-strand	45-47	3	2
β-strand	48-51	4	4
β-strand	54-57	4	4
α-helix	60-62	3
β-strand	63-66	4	3
β-strand	68	1	5
α-helix	69-74	6
β-strand	78-80	3	6
β-strand	88	1	5
β-strand	92-94	3	7
β-strand	95-97	3	6
α-helix	98	1
β-strand	102-104	3	8
β-strand	108-110	3	7
β-strand	111-114	4	9
β-strand	117-120	4	9
α-helix	123-125	3
β-strand	126-128	3	8

Chain Q: 4 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	10
α-helix	7-9	3
β-strand	16-19	4	11
β-strand	25	1	10
β-strand	29-34	6	11
β-strand	38-41	4	12
β-strand	45-47	3	11
β-strand	48-51	4	13
β-strand	54-57	4	13
β-strand	63-66	4	12
β-strand	68	1	14
α-helix	71-74	4
β-strand	78-80	3	15
β-strand	88	1	14
β-strand	92-94	3	16
β-strand	95-97	3	15
α-helix	98	1
β-strand	102-104	3	17
β-strand	108-110	3	16
β-strand	111-114	4	18
β-strand	117-120	4	18
α-helix	123-125	3
β-strand	126-128	3	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement decay-accelerating factor	P, Q	protein	125	HOMO SAPIENS	P08174 (AlphaFold model)

Sequence of entity 1 (P, Q), FASTA

>1H03_1 COMPLEMENT DECAY-ACCELERATING FACTOR (chains P, Q)
KSCPNPGEIRNGQIDVPGGILFGATISFSCNTGYKLFGSTSSFCLISGSSVQWSDPLPEC
REIYCPAPPQIDNGIIQGERDHYGYRQSVTYACNKGFTMIGEHSIYCTVNNDEGEWSGPP
PECRG

Primary citation

Mapping Cd55 Function. The Structure of Two Pathogen-Binding Domains at 1.7 A. Williams, P., Chaudhry, Y., Goodfellow, I. et al. J Biol Chem (2003) 278:10691. DOI 10.1074/JBC.M212561200 · PubMed

Other PDB entries of the same protein (UniProt P08174 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1H04 2.0 Å, Human CD55 domains 3 & 4
1OK3 2.2 Å, Decay accelerating factor (cd55): the structure of an intact human complement regulator.
1OJV 2.3 Å, Decay accelerating factor (CD55): the structure of an intact human complement regulator.
1OJW 2.3 Å, Decay accelerating factor (CD55): the structure of an intact human complement regulator.
1OK2 2.5 Å, Decay accelerating factor (CD55): the structure of an intact human complement regulator.
1OJY 2.6 Å, Decay accelerating factor (cd55): the structure of an intact human complement regulator.
1OK1 2.6 Å, Decay accelerating factor (cd55) : the structure of an intact human complement regulator.
8K9T 2.66 Å, Cryo-EM structure of the products-bound PGAP1(Bst1)-S327A from Chaetonium thermophilum
8K9R 2.68 Å, Cryo EM structure of the products-bound PGAP1(Bst1)-H443N from Chaetomium thermophilum
1H2P 2.8 Å, Human CD55 domains 3 & 4
6LA5 2.86 Å, Cryo-EM structure of echovirus 11 complexed with its attaching receptor CD55 at pH 7.4
1H2Q 3.0 Å, Human CD55 domains 3 & 4

Browse structure collections

About this viewer

MolViewer shows 1H03 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.