5FMV: Human CD45 extracellular region, domains d1-d4

Crystal structure of human CD45 extracellular region, domains d1-d4. Determined by X-ray diffraction at 2.9 Å resolution. Released 23 Mar 2016.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
5,811
Mol. weight
86.21 kDa
Ligands
NAG
Released
23 Mar 2016

Explore 5FMV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5FMV contains 25 α-helices and 62 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: 12 helices, 32 β-strands

ElementResiduesLengthSheet
β-strand22511
α-helix226-2294
β-strand235-24062
β-strand245-25062
β-strand257-25823
β-strand267-27152
α-helix2721
β-strand276-28273
β-strand28711
α-helix2901
β-strand291-29663
α-helix301-3033
β-strand304-30854
α-helix312-3143
β-strand319-32574
α-helix333-3353
β-strand336-34275
β-strand345-34845
β-strand351-35444
α-helix357-3582
β-strand362-371105
β-strand374-384115
β-strand394-39966
β-strand406-41166
β-strand419-42577
β-strand429-43687
β-strand441-44446
α-helix447-4482
β-strand452-462117
β-strand466-46837
β-strand472-47767
α-helix478-4803
α-helix482-4865
β-strand487-49378
β-strand499-50468
β-strand516-52279
β-strand526-53279
β-strand536-53948
α-helix542-5432
β-strand547-55489
β-strand555110
β-strand560110
α-helix561-5633
β-strand564-56969
Chain B: 13 helices, 30 β-strands
ElementResiduesLengthSheet
β-strand235-240611
β-strand245-250611
β-strand257-258212
α-helix264-2663
β-strand267-271511
α-helix2721
β-strand276-282712
α-helix2871
α-helix2901
β-strand291-296612
α-helix301-3033
β-strand304-308513
α-helix312-3143
β-strand319-325713
α-helix333-3353
β-strand336-342714
β-strand345-348414
β-strand351-354413
α-helix357-3582
β-strand362-3711014
β-strand374-3841114
β-strand394-399615
β-strand406-411615
β-strand419-42577
β-strand430-43677
β-strand441-444415
α-helix447-4482
β-strand452-462117
β-strand466-46837
β-strand472-47767
α-helix478-4803
α-helix482-4865
β-strand487-493716
β-strand499-504616
β-strand516-522717
β-strand526-532717
β-strand536-539416
α-helix542-5432
β-strand547-554817
β-strand555118
β-strand560118
α-helix561-5633
β-strand564-569617

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Receptor-type tyrosine-protein phosphatase CA, Bprotein361HOMO SAPIENSP08575 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5FMV_1 RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE C (chains A, B)
ETGKPTCDEKYANITVDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASV
SISHNSCTAPDKTLILDVPPGVEKFQLHDCTQVEKADTTICLKWKNIETFTCDTQNITYR
FQCGNMIFDNKEIKLENLEPEHEYKCDSEILYNNHKFTNASKIIKTDFGSPGEPQIIFCR
SEAAHQGVITWNPPQRSFHNFTLCYIKETEKDCLNLDKNLIKYDLQNLKPYTKYVLSLHA
YIIAKVQRNGSAAMCHFTTKSAPPSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLE
VEAGNTLVRNESHKNCDFRVKDLQYSTDYTFKAYFHNGDYPGEPFILHHSTSGTKHHHHH
H

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O611

Water and common crystallization additives (SO4) are not listed.

Primary citation

Initiation of T Cell Signaling by Cd45 Segregation at 'Close Contacts'. Chang, V.T., Fernandes, R.A., Ganzinger, K.A. et al. Nat Immunol (2016) 17:574. DOI 10.1038/NI.3392 · PubMed

Other PDB entries of the same protein (UniProt P08575 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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