4LCJ: CtBP2

CtBP2 in complex with substrate MTOB. Determined by X-ray diffraction at 2.86 Å resolution. Released 19 Mar 2014.

Method: X-ray diffraction
Resolution: 2.86 Å
Organism: Homo sapiens
Chains: 8
Atoms: 20,058
Mol. weight: 314.65 kDa
Ligands: KMT, NAD
Released: 19 Mar 2014

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

Secondary structure: helices and β-sheets

4LCJ contains 152 α-helices and 136 β-strands across 8 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: 19 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	35-38	4	1
α-helix	47-51	5
β-strand	56-59	4	1
α-helix	65-67	3
α-helix	70-75	6
β-strand	76-81	6	1
β-strand	87	1	2
α-helix	89-93	5
β-strand	100-103	4	1
β-strand	111	1	2
α-helix	113-118	6
β-strand	122-124	3	1
α-helix	131-147	17
α-helix	149-157	9
α-helix	165-171	7
β-strand	182-186	5	3
α-helix	190-199	10
α-helix	200-202	3
α-helix	204	1
β-strand	205-209	5	3
α-helix	214	1
α-helix	217-220	4
β-strand	224-226	3	3
α-helix	229-235	7
β-strand	238-241	4	3
β-strand	253	1	4
α-helix	255-258	4
α-helix	262	1
β-strand	265-269	5	3
α-helix	273-275	3
β-strand	276	1	4
α-helix	278-287	10
β-strand	290-295	6	3
β-strand	316-318	3	3
α-helix	327-346	20
β-strand	356	1	1

Chain B: 18 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	35-38	4	5
α-helix	47-51	5
β-strand	56-59	4	5
α-helix	65-67	3
α-helix	70-75	6
β-strand	76-81	6	5
β-strand	87	1	6
α-helix	89-93	5
β-strand	100-103	4	5
β-strand	111	1	6
α-helix	113-118	6
β-strand	122-124	3	5
α-helix	131-147	17
α-helix	149-157	9
α-helix	165-171	7
β-strand	182-186	5	7
α-helix	190-199	10
α-helix	200-202	3
β-strand	205-209	5	7
α-helix	214	1
α-helix	217-220	4
β-strand	224-225	2	7
α-helix	229-235	7
β-strand	238-241	4	7
β-strand	253	1	8
α-helix	255-258	4
α-helix	262	1
β-strand	265-269	5	7
α-helix	273-275	3
β-strand	276	1	8
α-helix	278-286	9
β-strand	290-295	6	7
β-strand	316-318	3	7
α-helix	327-346	20
β-strand	356	1	5

Chain C: 19 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	35-38	4	9
α-helix	47-51	5
β-strand	56-59	4	9
α-helix	65-67	3
α-helix	70-75	6
β-strand	76-81	6	9
β-strand	87	1	10
α-helix	89-93	5
β-strand	100-103	4	9
β-strand	111	1	10
α-helix	113-118	6
β-strand	122-124	3	9
α-helix	131-147	17
α-helix	149-157	9
α-helix	165-171	7
β-strand	182-186	5	11
α-helix	190-199	10
α-helix	200-202	3
α-helix	204	1
β-strand	205-209	5	11
α-helix	214	1
α-helix	217-220	4
β-strand	224-225	2	11
α-helix	229-235	7
β-strand	238-241	4	11
β-strand	253	1	12
α-helix	255-258	4
α-helix	262	1
β-strand	265-269	5	11
α-helix	273-275	3
β-strand	276	1	12
α-helix	278-286	9
β-strand	290-295	6	11
β-strand	316-318	3	11
α-helix	327-346	20
β-strand	356	1	9

Chain D: 19 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	35-38	4	13
α-helix	47-51	5
β-strand	56-59	4	13
α-helix	65-67	3
α-helix	70-75	6
β-strand	76-81	6	13
β-strand	87	1	14
α-helix	89-93	5
β-strand	100-103	4	13
β-strand	111	1	14
α-helix	113-118	6
β-strand	122-125	4	13
α-helix	131-147	17
α-helix	149-157	9
α-helix	165-171	7
β-strand	182-186	5	15
α-helix	190-199	10
α-helix	200-202	3
α-helix	204	1
β-strand	205-209	5	15
α-helix	214	1
α-helix	217-220	4
β-strand	224-225	2	15
α-helix	229-235	7
β-strand	238-241	4	15
β-strand	253	1	16
α-helix	255-258	4
α-helix	262	1
β-strand	265-269	5	15
α-helix	273-275	3
β-strand	276	1	16
α-helix	278-286	9
β-strand	290-295	6	15
β-strand	316-318	3	15
α-helix	327-346	20
β-strand	356	1	13

Chain E: 20 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	35-38	4	17
α-helix	47-52	6
β-strand	56-59	4	17
α-helix	65-67	3
α-helix	70-75	6
β-strand	76-81	6	17
β-strand	87	1	18
α-helix	89-93	5
β-strand	100-103	4	17
β-strand	111	1	18
α-helix	113-118	6
β-strand	122-124	3	17
α-helix	131-147	17
α-helix	149-157	9
α-helix	165-171	7
β-strand	182-186	5	19
α-helix	190-199	10
α-helix	200-202	3
α-helix	204	1
β-strand	205-209	5	19
α-helix	214	1
α-helix	217-220	4
β-strand	224-225	2	19
α-helix	229-235	7
β-strand	238-241	4	19
α-helix	244-245	2
β-strand	253	1	20
α-helix	255-258	4
α-helix	262	1
β-strand	265-269	5	19
α-helix	273-275	3
β-strand	276	1	20
α-helix	278-286	9
β-strand	290-295	6	19
β-strand	316-318	3	19
α-helix	327-346	20
β-strand	356	1	17

Chain F: 19 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	35-38	4	21
α-helix	48-51	4
β-strand	56-59	4	21
α-helix	65-67	3
α-helix	70-75	6
β-strand	76-81	6	21
β-strand	87	1	22
α-helix	89-94	6
β-strand	100-103	4	21
β-strand	111	1	22
α-helix	113-118	6
β-strand	122-124	3	21
α-helix	131-147	17
α-helix	149-157	9
α-helix	165-171	7
β-strand	182-186	5	23
α-helix	190-199	10
α-helix	200-202	3
α-helix	204	1
β-strand	205-209	5	23
α-helix	214	1
α-helix	217-220	4
β-strand	224-225	2	23
α-helix	229-235	7
β-strand	238-241	4	23
β-strand	253	1	24
α-helix	255-258	4
α-helix	262	1
β-strand	265-269	5	23
α-helix	273-275	3
β-strand	276	1	24
α-helix	278-287	10
β-strand	290-295	6	23
β-strand	316-318	3	23
α-helix	327-346	20
β-strand	356	1	21

Chain G: 19 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	36-38	3	25
α-helix	48-51	4
β-strand	57-59	3	25
α-helix	65-67	3
α-helix	70-74	5
β-strand	78-81	4	25
β-strand	87	1	26
α-helix	89-93	5
β-strand	101-103	3	25
β-strand	111	1	26
α-helix	113-118	6
β-strand	123-124	2	25
α-helix	131-147	17
α-helix	149-157	9
α-helix	165-171	7
β-strand	182-186	5	27
α-helix	190-199	10
α-helix	200-202	3
α-helix	204	1
β-strand	205-209	5	27
α-helix	214	1
α-helix	217-220	4
β-strand	224-225	2	27
α-helix	229-235	7
β-strand	238-241	4	27
β-strand	253	1	28
α-helix	255-259	5
α-helix	262	1
β-strand	265-269	5	27
α-helix	273-275	3
β-strand	276	1	28
α-helix	278-287	10
β-strand	290-295	6	27
β-strand	316-318	3	27
α-helix	327-345	19
β-strand	356	1	25

Chain H: 19 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	35-38	4	29
α-helix	48-51	4
β-strand	56-59	4	29
α-helix	65-67	3
α-helix	70-75	6
β-strand	76-81	6	29
β-strand	87	1	30
α-helix	89-94	6
β-strand	100-103	4	29
β-strand	111	1	30
α-helix	113-118	6
β-strand	122-124	3	29
α-helix	131-147	17
α-helix	149-157	9
α-helix	165-171	7
β-strand	182-186	5	31
α-helix	190-199	10
α-helix	200-202	3
α-helix	204	1
β-strand	205-209	5	31
α-helix	214	1
α-helix	217-220	4
β-strand	224-226	3	31
α-helix	229-235	7
β-strand	238-241	4	31
β-strand	253	1	32
α-helix	255-258	4
α-helix	262	1
β-strand	265-269	5	31
α-helix	273-275	3
β-strand	276	1	32
α-helix	278-286	9
β-strand	290-295	6	31
β-strand	316-318	3	31
α-helix	327-346	20
β-strand	356	1	29

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
C-terminal-binding protein 2	A, B, C, D, E, F, G, H	protein	349	Homo sapiens	P56545 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>4LCJ_1 C-terminal-binding protein 2 (chains A, B, C, D, E, F, G, H)
GSHMASMTGGQQMGRGSHPRPLVALLDGRDCTVEMPILKDLATVAFCDAQSTQEIHEKVL
NEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEE
TADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREVASGAARIRGETLGLIGFGRTGQ
AVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLI
NDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDA
PNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPESLRNCVNKEFF

Ligands and cofactors

ID	Name	Formula	Copies
KMT	4-(methylsulfanyl)-2-oxobutanoic acid	C5 H8 O3 S	8
NAD	Nicotinamide-adenine-dinucleotide	C21 H27 N7 O14 P2	8

Primary citation

Crystal structures of human CtBP in complex with substrate MTOB reveal active site features useful for inhibitor design. Hilbert, B.J., Grossmann, S.R., Schiffer, C.A. et al. FEBS Lett (2014) 588:1743-1748. DOI 10.1016/j.febslet.2014.03.026 · PubMed

Other PDB entries of the same protein (UniProt P56545 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9WRI 1.85 Å, Crystal structure of CtBP2 in complex with G9a
8ATI 2.6 Å, Human CtBP2(31-364) in complex with RAI2 peptide(315-322)
2OME 2.8 Å, Crystal structure of human CTBP2 dehydrogenase complexed with NAD(H)
6WKW 3.6 Å, EM structure of CtBP2 with a minimal dehydrogenase domain of CtBP2

Browse structure collections

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