2SRC: Human tyrosine-protein kinase C-src

Crystal structure of human tyrosine-protein kinase C-src, in complex with AMP-pnp. Determined by X-ray diffraction at 1.5 Å resolution. Released 22 Jul 1999.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Homo sapiens
Chains
1
Atoms
3,915
Mol. weight
52.22 kDa
Ligands
ANP
Released
22 Jul 1999

Explore 2SRC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2SRC contains 26 α-helices and 26 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: 26 helices, 26 β-strands

ElementResiduesLengthSheet
β-strand86-8831
β-strand9212
β-strand9911
β-strand10212
β-strand107-11261
β-strand118-12361
β-strand129-13351
α-helix134-1363
β-strand137-13931
β-strand14913
α-helix155-1628
α-helix167-1682
β-strand171-17663
β-strand184-19293
β-strand196-20493
β-strand205-20624
β-strand212-21324
β-strand219-22024
α-helix223-2297
β-strand243-24423
α-helix245-2462
α-helix248-2525
β-strand26115
α-helix264-2663
β-strand267-27595
β-strand279-28685
β-strand290-29785
α-helix304-31512
β-strand32216
α-helix323-3242
β-strand325-32955
α-helix3341
β-strand335-33845
β-strand34516
α-helix346-3505
α-helix360-37920
α-helix389-3913
β-strand392-39546
α-helix396-3983
β-strand399-40246
α-helix407-4104
α-helix414-4174
α-helix426-4283
α-helix431-4366
α-helix441-45515
α-helix460-4612
α-helix468-4769
α-helix481-4844
α-helix489-49810
α-helix503-5053
α-helix507-5082
α-helix509-5179

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tyrosine-protein kinase srcAprotein452Homo sapiensP12931 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2SRC_1 TYROSINE-PROTEIN KINASE SRC (chains A)
MVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSD
SIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKH
YKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWE
IPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEK
LVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMN
YVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTI
KSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRK
EPEERPTFEYLQAFLEDYFTSTEPQYQPGENL

Ligands and cofactors

IDNameFormulaCopies
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P31

Primary citation

Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Xu, W., Doshi, A., Lei, M. et al. Mol Cell (1999) 3:629-638. DOI 10.1016/S1097-2765(00)80356-1 · PubMed

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

Browse structure collections

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