2K5B: Human CDC37-HSP90 docking model based on NMR

Human CDC37-HSP90 docking model based on NMR. Determined by solution NMR. Released 9 Dec 2008.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 2,742
Mol. weight: 39.06 kDa
Released: 9 Dec 2008

Explore 2K5B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2K5B contains 20 α-helices and 8 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, 8 β-strands

Element	Residues	Length	Sheet
β-strand	18-21	4	1
α-helix	22-23	2
α-helix	24-35	12
α-helix	43-65	23
α-helix	67-70	4
β-strand	78-83	6	1
β-strand	88-93	6	1
α-helix	100-104	5
α-helix	105-109	5
α-helix	113-124	12
α-helix	128-130	3
α-helix	139-143	5
β-strand	145-153	9	1
β-strand	159-164	6	1
β-strand	169-174	6	1
α-helix	178-179	2
β-strand	183-190	8	1
α-helix	196-198	3
α-helix	200-210	11
β-strand	218-220	3	1

Chain B: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	149-162	14
α-helix	168-177	10
α-helix	179-181	3
α-helix	184-199	16
α-helix	203-226	24
α-helix	230-232	3
α-helix	236-239	4
α-helix	246-275	30

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Heat shock protein HSP 90-alpha	A	protein	210	Homo sapiens	P07900 (AlphaFold model)
Hsp90 co-chaperone Cdc37	B	protein	129	Homo sapiens	Q16543 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2K5B_1 Heat shock protein HSP 90-alpha (chains A)
EEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYETLTDPSKLDSG
KELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQ
FGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKED
QTEYLEERRIKEIVKKHSQFIGYPITLFVE

Sequence of entity 2 (B), FASTA

>2K5B_2 Hsp90 co-chaperone Cdc37 (chains B)
HKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALME
QVAHQTIVMQFILELAKSLKVDPRACFRQFFTKIKTADRQYMEGFNDELEAFKERVRGRA
KLRIEKAMK

Primary citation

The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy. Sreeramulu, S., Jonker, H.R.A., Langer, T. et al. J Biol Chem (2009) 284:3885-3896. DOI 10.1074/jbc.M806715200 · PubMed

Other PDB entries of the same protein (UniProt P07900 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6TN5 1.17 Å, Rapid optimisation of fragments and hits to lead compounds from screening of crude…
5J80 1.17 Å, Crystal Structure of Apo Hsp90-alpha N-domain L107A mutant
3T0H 1.2 Å, Structure insights into mechanisms of ATP hydrolysis and the activation of human Hsp90
5J2X 1.22 Å, Crystal Structure of Hsp90-alpha N-domain in complex with…
3T10 1.24 Å, HSP90 N-terminal domain bound to ACP
6TN4 1.27 Å, Rapid optimisation of fragments and hits to lead compounds from screening of crude…
3WHA 1.3 Å, Hsp90 alpha N-terminal domain in complex with a tricyclic inhibitor
5XRD 1.3 Å, Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FS7
2YK9 1.32 Å, Tricyclic series of Hsp90 inhibitors
5LRL 1.33 Å, Crystal structure of HSP90 in complex with A003492875
6GR5 1.34 Å, Structure of human Heat shock protein 90-alpha N-terminal domain (Hsp90-NTD) variant…
3B28 1.35 Å, Hsp90 alpha N-terminal domain in complex with an inhibitor CH5015765

Browse structure collections

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