1FMK: Human tyrosine-protein kinase C-src

Crystal structure of human tyrosine-protein kinase C-src. Determined by X-ray diffraction at 1.5 Å resolution. Released 20 Aug 1997.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 4,006
Mol. weight: 51.71 kDa
Released: 20 Aug 1997

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

Secondary structure: helices and β-sheets

1FMK contains 21 α-helices and 28 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: 21 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	83	1
β-strand	84-88	5	1
β-strand	92	1	2
β-strand	99	1	1
β-strand	102	1	2
β-strand	107-110	4	1
β-strand	118-123	6	1
β-strand	129-133	5	1
α-helix	134-136	3
β-strand	137-139	3	1
α-helix	143-145	3
β-strand	149-151	3	3
α-helix	155-162	8
β-strand	171-176	6	3
β-strand	184-192	9	3
β-strand	196-204	9	3
β-strand	205-206	2	4
β-strand	212-213	2	4
β-strand	219-220	2	4
α-helix	223-230	8
β-strand	235	1	5
β-strand	237	1	5
β-strand	243-244	2	3
α-helix	245-246	2
β-strand	261	1	6
α-helix	264-266	3
β-strand	267-275	9	6
β-strand	280-286	7	6
β-strand	290-296	7	6
α-helix	304-316	13
β-strand	322	1	7
β-strand	325-329	5	6
β-strand	335-338	4	6
β-strand	345	1	7
α-helix	346-350	5
α-helix	352-355	4
α-helix	360-379	20
α-helix	389-391	3
β-strand	392-394	3	7
α-helix	396-398	3
β-strand	400-402	3	7
α-helix	426-428	3
α-helix	431-436	6
α-helix	441-456	16
α-helix	460-461	2
α-helix	468-476	9
α-helix	489-498	10
α-helix	503-505	3
α-helix	509-517	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine-protein kinase src	A	protein	452	Homo sapiens	P12931 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1FMK_1 TYROSINE-PROTEIN KINASE SRC (chains A)
MVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSD
SIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKH
YKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWE
IPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEK
LVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMN
YVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTI
KSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRK
EPEERPTFEYLQAFLEDYFTSTEPQYQPGENL

Primary citation

Three-dimensional structure of the tyrosine kinase c-Src. Xu, W., Harrison, S.C., Eck, M.J. Nature (1997) 385:595-602. DOI 10.1038/385595a0 · PubMed

Other PDB entries of the same protein (UniProt P12931 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9OFX 1.45 Å, Crystal structure of c-Src SH3 domain in H32 space group mediated by nickel
1O43 1.5 Å, Crystal structure of SH2 in complex with RU82129.
1O4A 1.5 Å, Crystal structure of SH2 in complex with RU82197.
1O4R 1.5 Å, Crystal structure of SH2 in complex with RU78783.
2SRC 1.5 Å, Crystal structure of human tyrosine-protein kinase C-src, in complex with AMP-pnp
6C4S 1.5 Å, Human cSrc SH3 Domain in complex with Choline Kinase fragment 60-69
7NG7 1.5 Å, Src kinase bound to eCF506 trapped in inactive conformation
8VCF 1.5 Å, Crystal structure of Superbinder Src SH2 domain with Cysteine to Serine mutations
1O48 1.55 Å, Crystal structure of SH2 in complex with RU85053.
1O4G 1.55 Å, Crystal structure of SH2 in complex with DPI59.
1O4K 1.57 Å, Crystal structure of SH2 in complex with pasbn.
4F5B 1.57 Å, Triple mutant Src SH2 domain bound to phosphotyrosine

Browse structure collections

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