1ECD: Erythrocruorin in different ligand states

Structure of erythrocruorin in different ligand states refined at 1.4 Å resolution. Determined by X-ray diffraction at 1.4 Å resolution. Released 5 Jul 1979.

Method: X-ray diffraction
Resolution: 1.4 Å
Organism: Chironomus thummi thummi
Chains: 1
Atoms: 1,186
Mol. weight: 15.42 kDa
Ligands: HEM
Released: 5 Jul 1979

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

Secondary structure: helices and β-sheets

1ECD contains 10 α-helices and 0 β-strands across 1 chain. 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	3-14	12
α-helix	20-30	11
α-helix	32-35	4
α-helix	46-49	4
α-helix	53-71	19
α-helix	77-87	11
α-helix	88-90	3
α-helix	94-111	18
α-helix	114-117	4
α-helix	118-135	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Erythrocruorin (aquo met)	A	protein	136	Chironomus thummi thummi	P02229 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1ECD_1 ERYTHROCRUORIN (AQUO MET) (chains A)
LSADQISTVQASFDKVKGDPVGILYAVFKADPSIMAKFTQFAGKDLESIKGTAPFETHAN
RIVGFFSKIIGELPNIEADVNTFVASHKPRGVTHDQLNNFRAGFVSYMKAHTDFAGAEAA
WGATLDTFFGMIFSKM

Ligands and cofactors

ID	Name	Formula	Copies
HEM	Protoporphyrin IX containing FE	C34 H32 Fe N4 O4	1

Primary citation

Structure of erythrocruorin in different ligand states refined at 1.4 A resolution. Steigemann, W., Weber, E. J Mol Biol (1979) 127:309-338. DOI 10.1016/0022-2836(79)90332-2 · PubMed

Other PDB entries of the same protein (UniProt P02229 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1ECA 1.4 Å, Structure of erythrocruorin in different ligand states refined at 1.4 Å resolution
1ECN 1.4 Å, Structure of erythrocruorin in different ligand states refined at 1.4 Å resolution
1ECO 1.4 Å, Structure of erythrocruorin in different ligand states refined at 1.4 Å resolution

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