4XAJ: Human NR2E1/TLX

Crystal structure of human NR2E1/TLX. Determined by X-ray diffraction at 3.55 Å resolution. Released 4 Mar 2015.

Method: X-ray diffraction
Resolution: 3.55 Å
Organisms: Escherichia coli O157:H7, Homo sapiens, DROSOPHILA MELANOGASTER
Chains: 6
Atoms: 18,097
Mol. weight: 259.71 kDa
Released: 4 Mar 2015

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

Secondary structure: helices and β-sheets

4XAJ contains 153 α-helices and 94 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: 37 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
α-helix	19-33	15
β-strand	36-40	5	1
α-helix	45-53	9
β-strand	61-65	5	1
α-helix	66-68	3
α-helix	69-74	6
β-strand	78-79	2	1
α-helix	80-81	2
α-helix	85-88	4
β-strand	91	1	2
α-helix	93-98	6
β-strand	100-101	2	3
β-strand	104-105	2	3
β-strand	107-113	7	1
β-strand	116-120	5	4
β-strand	130	1	5
α-helix	134-142	9
β-strand	147-149	3	4
α-helix	156-165	10
β-strand	169-174	6	6
β-strand	177-184	8	6
α-helix	188-202	15
α-helix	212-220	9
β-strand	224-229	6	4
α-helix	231-233	3
α-helix	234-238	5
β-strand	244-247	4	4
α-helix	248-250	3
β-strand	251	1	5
β-strand	252	1	7
β-strand	255	1	7
α-helix	256-257	2
β-strand	260-261	2	8
β-strand	262-269	8	1
α-helix	275-281	7
α-helix	282-286	5
α-helix	289-298	10
β-strand	303-304	2	1
β-strand	306	1	2
α-helix	307-313	7
α-helix	317-328	12
β-strand	330-331	2	8
α-helix	332-333	2
α-helix	338-353	16
α-helix	359-362	4
α-helix	363-365	3
α-helix	366-370	5
α-helix	1186-1201	16
α-helix	1206-1208	3
α-helix	1211-1233	23
α-helix	1242-1245	4
α-helix	1258-1277	20
α-helix	1282-1293	12
α-helix	1306-1308	3
α-helix	1311-1332	22
α-helix	1339-1346	8
α-helix	1347-1352	6
α-helix	1355-1362	8
α-helix	1370-1382	13

Chain B: 38 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	18
α-helix	19-33	15
β-strand	36-40	5	18
α-helix	45-53	9
β-strand	61-65	5	18
α-helix	66-68	3
α-helix	69-74	6
β-strand	78	1	19
α-helix	79-81	3
α-helix	85-88	4
β-strand	91	1	20
α-helix	93-98	6
β-strand	100-101	2	21
β-strand	104-105	2	21
β-strand	108-113	6	18
β-strand	116-120	5	22
β-strand	130	1	23
α-helix	134-142	9
β-strand	147-149	3	22
α-helix	156-158	3
α-helix	160-165	6
β-strand	171-174	4	24
β-strand	177-183	7	24
α-helix	188-202	15
α-helix	212-220	9
β-strand	224-229	6	22
α-helix	231-233	3
α-helix	234-238	5
β-strand	244-247	4	22
α-helix	248-250	3
β-strand	251	1	23
β-strand	252	1	25
β-strand	255	1	25
α-helix	256-257	2
α-helix	259	1
β-strand	260-261	2	26
β-strand	262-268	7	18
β-strand	269	1	19
α-helix	275-281	7
α-helix	282-286	5
α-helix	289-296	8
β-strand	303-304	2	18
β-strand	306	1	20
α-helix	307-313	7
α-helix	317-328	12
β-strand	330-331	2	26
α-helix	332-333	2
α-helix	338-353	16
α-helix	359-362	4
α-helix	363-367	5
α-helix	373-1182	3
α-helix	1186-1202	17
α-helix	1204-1207	4
α-helix	1211-1232	22
α-helix	1241-1246	6
α-helix	1257-1277	21
α-helix	1282-1293	12
α-helix	1311-1332	22
α-helix	1338-1346	9
α-helix	1347-1352	6
α-helix	1355-1362	8
α-helix	1370-1379	10

Chain C: 37 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	8-13	6	9
α-helix	19-31	13
β-strand	36-40	5	9
α-helix	45-53	9
β-strand	61-65	5	9
α-helix	66-68	3
α-helix	69-74	6
β-strand	78	1	10
α-helix	79-81	3
α-helix	85-88	4
β-strand	91	1	11
α-helix	93-98	6
β-strand	100-101	2	12
β-strand	104-105	2	12
β-strand	107-113	7	9
β-strand	116-120	5	13
β-strand	130	1	14
α-helix	134-142	9
β-strand	147-149	3	13
α-helix	156-163	8
β-strand	169-174	6	15
β-strand	177-184	8	15
α-helix	188-202	15
α-helix	212-220	9
β-strand	224-229	6	13
α-helix	231-233	3
α-helix	234-237	4
β-strand	244-247	4	13
α-helix	248-250	3
β-strand	251	1	14
β-strand	252	1	16
β-strand	255	1	16
α-helix	259	1
β-strand	260-261	2	17
β-strand	262-268	7	9
β-strand	269	1	10
α-helix	275-280	6
α-helix	281-286	6
α-helix	289-296	8
β-strand	304	1	9
β-strand	306	1	11
α-helix	307-313	7
α-helix	317-328	12
β-strand	330-331	2	17
α-helix	332-333	2
α-helix	338-354	17
α-helix	362-368	7
α-helix	374-1202	22
α-helix	1204-1207	4
α-helix	1211-1232	22
α-helix	1240	1
α-helix	1241-1246	6
α-helix	1247-1251	5
α-helix	1257-1277	21
α-helix	1282-1293	12
α-helix	1306-1308	3
α-helix	1311-1332	22
α-helix	1338-1346	9
α-helix	1347-1352	6
α-helix	1355-1362	8
α-helix	1370-1379	10

Chain D: 38 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	9-12	4	27
α-helix	19-33	15
β-strand	37-40	4	27
α-helix	45-53	9
β-strand	61-65	5	27
α-helix	66-68	3
α-helix	69-74	6
β-strand	78-79	2	27
α-helix	80-81	2
α-helix	85-88	4
β-strand	91	1	28
α-helix	93-98	6
β-strand	100-101	2	29
β-strand	104-105	2	29
β-strand	107-113	7	27
β-strand	116-120	5	30
β-strand	130	1	31
α-helix	131-133	3
α-helix	134-142	9
β-strand	147-149	3	30
α-helix	156-163	8
β-strand	171-174	4	32
β-strand	177-183	7	32
α-helix	188-202	15
α-helix	212-220	9
β-strand	224-229	6	30
α-helix	231-233	3
α-helix	234-237	4
β-strand	244-247	4	30
α-helix	248-250	3
β-strand	251	1	31
β-strand	252	1	33
β-strand	255	1	33
α-helix	259	1
β-strand	260-261	2	34
β-strand	262-269	8	27
α-helix	275-280	6
α-helix	281-286	6
α-helix	289-296	8
β-strand	303-304	2	27
β-strand	306	1	28
α-helix	307-313	7
α-helix	317-327	11
β-strand	330-331	2	34
α-helix	332-333	2
α-helix	338-354	17
α-helix	362-368	7
α-helix	374-1202	22
α-helix	1204-1207	4
α-helix	1211-1232	22
α-helix	1240	1
α-helix	1241-1245	5
α-helix	1246-1251	6
α-helix	1255-1277	23
α-helix	1282-1293	12
α-helix	1306-1308	3
α-helix	1311-1332	22
α-helix	1338-1346	9
α-helix	1347-1352	6
α-helix	1355-1362	8
α-helix	1370-1379	10

Chain P: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1818-1827	10

Chain Q: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1818-1827	10
α-helix	1828-1830	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltose-binding periplasmic protein,Nuclear receptor subfamily 2 group E member 1	A, B, C, D	protein	576	Escherichia coli O157:H7, Homo sapiens	P0AEY0 (AlphaFold model), Q9Y466 (AlphaFold model)
Atrophin/grunge	P, Q	protein	18	DROSOPHILA MELANOGASTER	M9PHT1 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4XAJ_1 Maltose-binding periplasmic protein,Nuclear receptor subfamily 2 group E member 1 (chains A, B, C, D)
MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD
IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN
KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI
KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS
KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP
LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD
EALKDAQTNAAAEFTESVCESAARLLFMSIKWAKSVPAFSTLSLQDQLMLLEDAWRELFV
LGIAQWAIPVDANTLLAVSGMNGDNTDSQRLTLIISEIQALQEVVARFRQLRLDATEFAC
LKCIVTFKAVPTHSGSELRSFRNAAAIAALQDEAQLTLNSYIHTRYPTQPVRFGKLLLLL
PALRSISPSTIEEVFFKKTIGNVPITRLLSDMYKSS

Sequence of entity 2 (P, Q), FASTA

>4XAJ_2 Atrophin/grunge (chains P, Q)
YADTPALRQLSEYARPHV

Primary citation

Structural basis for corepressor assembly by the orphan nuclear receptor TLX. Zhi, X., Zhou, X.E., He, Y. et al. Genes Dev (2015) 29:440-450. DOI 10.1101/gad.254904.114 · PubMed

Other PDB entries of the same protein (UniProt P0AEY0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9PQP 1.07 Å, Crystal structure of maltose binding protein (Apo), mutant Trp340 to 4-Fluorotryptophan
9PQL 1.37 Å, Crystal structure of maltose binding protein (Apo), mutant Trp62 to 4-Fluorotryptophan
9PQN 1.37 Å, Crystal structure of maltose binding protein (Apo), mutant Trp340 to 4-Cyanotryptophan
9TY2 1.75 Å, Crystal structure of a Picomolar Nanobody in complex with Maltose Binding Protein, MBP,…
4WGI 1.85 Å, A Single Diastereomer of a Macrolactam Core Binds Specifically to Myeloid Cell Leukemia…
9PQK 1.87 Å, Crystal structure of maltose binding protein (Apo), mutant Trp10 to 4-Fluorotryptophan
4WVI 1.9 Å, Crystal structure of the Type-I signal peptidase from Staphylococcus aureus (SpsB) in…
4WVJ 1.95 Å, Crystal structure of the Type-I signal peptidase from Staphylococcus aureus (SpsB) in…
4YS9 2.0 Å, Ataxin-3 Carboxy-Terminal Region - Crystal C1 (tetragonal)
5II4 2.0 Å, Crystal structure of red abalone VERL repeat 1 with linker at 2.0 A resolution
5JON 2.04 Å, Crystal structure of the unliganded form of HCN2 CNBD
4WVG 2.05 Å, Crystal structure of the Type-I signal peptidase from Staphylococcus aureus (SpsB).

Browse structure collections

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