1I0E: Creatine kinase from human muscle

Crystal structure of creatine kinase from human muscle. Determined by X-ray diffraction at 3.5 Å resolution. Released 1 Apr 2003.

Method: X-ray diffraction
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 11,608
Mol. weight: 172.68 kDa
Released: 1 Apr 2003

Explore 1I0E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1I0E contains 60 α-helices and 81 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: 15 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	16-19	4
β-strand	27	1	1
β-strand	28	1	2
α-helix	29-33	5
α-helix	36-42	7
β-strand	46	1	3
β-strand	52	1	3
α-helix	53-62	10
β-strand	65	1	1
β-strand	71	1	2
α-helix	80-84	5
α-helix	86-93	8
β-strand	126-132	7	4
β-strand	135	1	4
β-strand	137	1	5
α-helix	148-164	17
α-helix	167-169	3
β-strand	171-175	5	4
α-helix	184-189	6
β-strand	216-220	5	4
β-strand	226-229	4	4
β-strand	235-242	8	4
α-helix	246-266	21
α-helix	270	1
β-strand	271	1	5
α-helix	272	1
β-strand	273-274	2	6
β-strand	278-279	2	6
α-helix	284-286	3
β-strand	288	1	6
β-strand	292-298	7	4
α-helix	308-315	8
β-strand	317-318	2	4
β-strand	333-338	6	4
α-helix	346-368	23

Chain B: 15 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	16-19	4
β-strand	27	1	7
β-strand	28	1	8
α-helix	29-33	5
α-helix	36-42	7
β-strand	46	1	9
β-strand	52	1	9
α-helix	53-62	10
β-strand	65	1	7
β-strand	71	1	8
α-helix	80-84	5
α-helix	86-96	11
β-strand	126-132	7	10
β-strand	135	1	10
β-strand	137	1	11
α-helix	148-164	17
α-helix	167-169	3
β-strand	171-175	5	10
α-helix	184-189	6
β-strand	216-220	5	10
β-strand	226-229	4	10
β-strand	235-242	8	10
α-helix	246-266	21
α-helix	270	1
β-strand	271	1	11
α-helix	272	1
β-strand	273-274	2	12
β-strand	278-279	2	12
α-helix	284-286	3
β-strand	288	1	12
β-strand	292-298	7	10
α-helix	308-315	8
β-strand	317	1	13
β-strand	333-337	5	10
β-strand	338	1	13
α-helix	346-368	23

Chains C and D: 15 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	16-19	4
β-strand	27	1	14
β-strand	28	1	15
α-helix	29-33	5
α-helix	36-42	7
β-strand	46	1	16
β-strand	52	1	16
α-helix	53-62	10
β-strand	65	1	14
β-strand	71	1	15
α-helix	80-84	5
α-helix	86-96	11
β-strand	126-133	8	17
β-strand	135	1	17
β-strand	137	1	18
α-helix	148-164	17
α-helix	167-169	3
β-strand	171-175	5	17
α-helix	184-189	6
β-strand	216-220	5	17
β-strand	226-229	4	17
β-strand	235-242	8	17
α-helix	246-266	21
α-helix	270	1
β-strand	271	1	18
α-helix	272	1
β-strand	273-274	2	19
β-strand	278-279	2	19
α-helix	284-286	3
β-strand	288	1	19
β-strand	291-298	8	17
α-helix	308-315	8
β-strand	317-318	2	17
β-strand	333-338	6	17
α-helix	346-368	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Creatine kinase,m chain	A, B, C, D	protein	381	Homo sapiens	P06732 (AlphaFold model)

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

>1I0E_1 CREATINE KINASE,M CHAIN (chains A, B, C, D)
MPFGNTHNKFKLNYKPEEEYPDLSKHNNHMAKVLTLELYKKLRDKETPSGFTVDDVIQTG
VDNPGHPFIMTVGCVAGDEESYEVFKELFDPIISDRHGGYKPTDKHKTDLNHENLKGGDD
LDPNYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKLSVEALNSLTGEFKGKYYPLKSMT
EKEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKSFLVWVNEEDHLRVISM
EKGGNMKEVFRRFCVGLQKIEEIFKKAGHPFMWNQHLGYVLTCPSNLGTGLRGGVHVKLA
HLSKHPKFEEILTRLRLQKRGTGGVDTAAVGSVFDVSNADRLGSSEVEQVQLVVDGVKLM
VEMEKKLEKGQSIDDMIPAQK

Primary citation

Structure of human muscle creatine kinase. Shen, Y.Q., Tang, L., Zhou, H.M. et al. Acta Crystallogr D Biol Crystallogr (2001) 57:1196-1200. DOI 10.1107/s0907444901007703 · PubMed

Other PDB entries of the same protein (UniProt P06732 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7BF2 1.43 Å, Ca2+-Calmodulin in complex with human muscle form creatine kinase peptide in extended…

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