5CBE: E10

E10 in complex with CXCL13. Determined by X-ray diffraction at 2.4 Å resolution. Released 4 Nov 2015.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Homo sapiens
Chains
6
Atoms
4,696
Mol. weight
76.01 kDa
Released
4 Nov 2015

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

Secondary structure: helices and β-sheets

5CBE contains 17 α-helices and 69 β-strands across 6 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: 3 helices, 14 β-strands

ElementResiduesLengthSheet
β-strand4-631
α-helix7-93
β-strand10-1232
β-strand18-2471
α-helix251
β-strand33-3972
β-strand45-5282
β-strand56-5942
β-strand67-7261
β-strand77-8261
α-helix84-863
β-strand88-9582
β-strand97-10043
β-strand100C-100F43
β-strand10312
β-strand10411
β-strand107-11152
Chain B: 2 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand414
β-strand515
β-strand9-1346
β-strand19-2465
β-strand33-3866
β-strand45-4846
β-strand4917
β-strand5317
α-helix54-552
β-strand62-6765
β-strand70-7565
α-helix80-823
β-strand85-9176
β-strand96-9836
β-strand9914
β-strand102-10656
Chain C: 2 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand5-628
α-helix7-93
β-strand10-1239
β-strand18-2368
β-strand33-3979
β-strand45-5289
β-strand56-5949
β-strand67-7268
β-strand77-8268
α-helix84-863
β-strand88-9589
β-strand97-99310
β-strand100D-100F310
β-strand10319
β-strand107-11159
Chain D: 3 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix2-32
β-strand4111
β-strand5112
β-strand9-12313
β-strand19-24612
β-strand33-38613
β-strand45-48413
β-strand49114
β-strand53114
α-helix54-552
β-strand62-67612
β-strand70-75612
α-helix80-823
β-strand85-91713
β-strand96-98313
β-strand99111
β-strand102-105413
Chain E: 3 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand5110
β-strand7115
β-strand11116
α-helix21-233
β-strand24-3073
β-strand33117
β-strand36117
β-strand40-4563
β-strand50-5343
α-helix58-614
α-helix62-654
Chain F: 4 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand7116
β-strand11115
β-strand15110
α-helix21-233
β-strand24-30710
α-helix31-322
α-helix391
β-strand40-45610
β-strand50-53410
α-helix58-6710

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E10 heavy chainA, Cprotein142Homo sapiensA0A0B4J2H0 (AlphaFold model)
E10 light chainB, Dprotein122Homo sapiensP01704 (AlphaFold model)
C-X-C motif chemokine 13E, Fprotein88Homo sapiensO43927 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>5CBE_1 E10 heavy chain (chains A, C)
QVQLVQSGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIPIFGTANY
AQKFQGRVTITADESTSTAYMELSSLRSEDTAVYYCAREPDYYDSSGYYPIDAFDIWGQG
TTVTVSSGGGGSGGGGSGGGGS
Sequence of entity 2 (B, D), FASTA
>5CBE_2 E10 light chain (chains B, D)
QSALTQPASVSASPGQSITISCTGTSSDVGAYDWVSWYQQHPGKAPKLLIFDVNNRPSGV
SHRFSGSKSGNTASLTISGLQAEDEADYYCASATLLDTYVFGTGTKVTVLGDQEPKSSDK
TH
Sequence of entity 3 (E, F), FASTA
>5CBE_3 C-X-C motif chemokine 13 (chains E, F)
MVLEVYYTSLRCRCVQESSVFIPRRFIDRIQILPRGNGCPRKEIIVWKKNKSIVCVDPQA
EWIQRMMEVLRKRSSSTLPVPVFKRKIP

Primary citation

A Combination of Structural and Empirical Analyses Delineates the Key Contacts Mediating Stability and Affinity Increases in an Optimized Biotherapeutic Single-chain Fv (scFv). Tu, C., Terraube, V., Tam, A.S. et al. J Biol Chem (2016) 291:1267-1276. DOI 10.1074/jbc.M115.688010 · PubMed

Other PDB entries of the same protein (UniProt A0A0B4J2H0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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