4NZW: STK25-MO25 Complex

Crystal Structure of STK25-MO25 Complex. Determined by X-ray diffraction at 3.58 Å resolution. Released 3 Dec 2014.

Method: X-ray diffraction
Resolution: 3.58 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,718
Mol. weight: 72.79 kDa
Ligands: J60
Released: 3 Dec 2014

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

Secondary structure: helices and β-sheets

4NZW contains 38 α-helices and 13 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: 23 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	12-26	15
α-helix	38-54	17
α-helix	66-77	12
α-helix	79-85	7
α-helix	92-106	15
β-strand	110	1	1
β-strand	113	1	1
α-helix	115-122	8
α-helix	125-132	8
α-helix	133-135	3
α-helix	137-140	4
α-helix	142-150	9
α-helix	154-161	8
α-helix	164-168	5
α-helix	169-172	4
β-strand	177	1	2
α-helix	182-193	12
α-helix	196-205	10
α-helix	207-217	11
α-helix	223-238	16
α-helix	243-249	7
α-helix	253-262	10
α-helix	268-283	16
α-helix	289-297	9
α-helix	299-307	9
α-helix	322-331	10

Chain B: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	16-18	3
β-strand	20-22	3	2
β-strand	34-39	6	2
β-strand	45-51	7	2
α-helix	61-63	3
α-helix	64-70	7
β-strand	78	1	3
β-strand	81-86	6	2
β-strand	91-95	5	2
β-strand	102	1	4
α-helix	114-133	20
β-strand	147-148	2	4
β-strand	154-155	2	4
β-strand	156	1	3
α-helix	179-181	3
α-helix	184-187	4
α-helix	195-210	16
α-helix	220-226	7
α-helix	231-233	3
α-helix	241-250	10
α-helix	255-257	3
α-helix	264-266	3
α-helix	268-272	5
α-helix	277-280	4
α-helix	281-290	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calcium-binding protein 39	A	protein	331	Homo sapiens	Q9Y376 (AlphaFold model)
Serine/threonine-protein kinase 25	B	protein	295	Homo sapiens	O00506 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4NZW_1 Calcium-binding protein 39 (chains A)
GAMASHKSPADIVKNLKESMAVLEKQDISDKKAEKATEEVSKNLVAMKEILYGTNEKEPQ
TEAVAQLAQELYNSGLLSTLVADLQLIDFEGKKDVAQIFNNILRRQIGTRTPTVEYICTQ
QNILFMLLKGYESPEIALNCGIMLRECIRHEPLAKIILWSEQFYDFFRYVEMSTFDIASD
AFATFKDLLTRHKLLSAEFLEQHYDRFFSEYEKLLHSENYVTKRQSLKLLGELLLDRHNF
TIMTKYISKPENLKLMMNLLRDKSRNIQFEAFHVFKVFVANPNKTQPILDILLKNQAKLI
EFLSKFQNDRTEDEQFNDEKTYLVKQIRDLK

Sequence of entity 2 (B), FASTA

>4NZW_2 Serine/threonine-protein kinase 25 (chains B)
QAMAHLRGFANQHSRVDPEELFTKLDRIGKGSFGEVYKGIDNHTKEVVAIKIIDLEEAED
EIEDIQQEITVLSQCDSPYITRYFGSYLKSTKLWIIMEYLGGGSALDLLKPGPLEETYIA
TILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLAAFGVAGQLTDTQIKRNTFVGT
PFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQ
HSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTSFLTELIDRYKRWKSE

Ligands and cofactors

ID	Name	Formula	Copies
J60	5-[(E)-(5-chloro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]-N-[2-(diethylamin…	C22 H27 Cl N4 O2	1

Primary citation

Structural insights into regulatory mechanisms of MO25-mediated kinase activation. Hao, Q., Feng, M., Shi, Z. et al. J Struct Biol (2014) 186:224-233. DOI 10.1016/j.jsb.2014.04.005 · PubMed

Other PDB entries of the same protein (UniProt Q9Y376 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1UPK 1.85 Å, Crystal structure of MO25 in complex with a C-terminal peptide of STRAD
3GNI 2.35 Å, Structure of STRAD and MO25
1UPL 2.6 Å, Crystal structure of MO25 alpha
2WTK 2.65 Å, Structure of the heterotrimeric LKB1-STRADalpha-MO25alpha complex
8VSU 2.86 Å, Cryo-EM structure of LKB1-STRADalpha-MO25alpha heterocomplex
4FZA 3.15 Å, Crystal structure of MST4-MO25 complex
4O27 3.19 Å, Crystal structure of MST3-MO25 complex with WIF motif
4FZD 3.25 Å, Crystal structure of MST4-MO25 complex with WSF motif
4FZF 3.64 Å, Crystal structure of MST4-MO25 complex with DKI

Browse structure collections

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