4ORA: Human calcineurin mutant

Crystal structure of a human calcineurin mutant. Determined by X-ray diffraction at 2.75 Å resolution. Released 20 May 2015.

Method
X-ray diffraction
Resolution
2.75 Å
Organism
Homo sapiens
Chains
2
Atoms
4,614
Mol. weight
80.9 kDa
Ligands
CA, FE, ZN
Released
20 May 2015

Explore 4ORA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ORA contains 34 α-helices and 22 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 A: 22 helices, 20 β-strands

ElementResiduesLengthSheet
α-helix16-194
α-helix21-233
α-helix31-344
α-helix371
β-strand3811
α-helix391
α-helix40-434
β-strand4412
β-strand5012
α-helix52-609
β-strand6511
α-helix67-8216
β-strand87-9043
β-strand94-9744
α-helix104-11411
β-strand122-12434
α-helix135-14814
β-strand153-15534
α-helix156-1583
α-helix163-1686
α-helix171-1788
α-helix181-19313
β-strand197-20043
β-strand204-20743
α-helix218-2225
α-helix235-2417
β-strand243-24425
β-strand257-25935
β-strand267-26935
α-helix271-28010
β-strand285-28843
β-strand297-29933
β-strand30216
β-strand30916
β-strand311-31443
α-helix320-3223
β-strand328-33474
β-strand337-34374
α-helix353-3553
α-helix358-37821
α-helix479-4846
α-helix487-4904
Chain B: 12 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix6-83
α-helix16-2914
α-helix39-435
α-helix46-483
α-helix54-618
α-helix71-799
α-helix87-9812
β-strand10617
α-helix108-11912
α-helix125-13915
β-strand14717
α-helix149-1568
α-helix157-1593
α-helix161-1633

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoformAprotein544Homo sapiensP16298 (AlphaFold model)
Calcineurin subunit B type 1Bprotein170Homo sapiensP63098 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4ORA_1 Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (chains A)
MGSSHHHHHHSSGLVPRGSHMAAPEPARAAPPPPPPPPPPPGADRVVKAVPFPPTHRLTS
EEVFDLDGIPRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDI
HGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNH
ECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDD
IRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQN
NNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNI
RQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLSICSDDELMTEGEDQFDGSAAA
RKEIIRNKIRAIGKMARYLSVLREESESVLTLKGLTPTGMLPSGVLAGGRQTLQSATVEA
IEAEKAIRGFSPPHRICSFEEAKGLDRINERMPPRKDAVQQDGFNSLNTAHATENHGTGN
HTAQ
Sequence of entity 2 (B), FASTA
>4ORA_2 Calcineurin subunit B type 1 (chains B)
MGNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVID
IFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMV
GNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4
FEFE (III) ionFe1
ZNZinc ionZn1

Primary citation

Cooperative autoinhibition and multi-level activation mechanisms of calcineurin. Li, S.J., Ma, L., Wang, J. et al. To be published.

Other PDB entries of the same protein (UniProt P16298 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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