2J3N: Human thioredoxin reductase 1

X-ray structure of human thioredoxin reductase 1. Determined by X-ray diffraction at 2.8 Å resolution. Released 3 Jul 2007.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: HOMO SAPIENS
Chains: 6
Atoms: 23,294
Mol. weight: 351.42 kDa
Ligands: FAD, NAP
Released: 3 Jul 2007

Explore 2J3N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2J3N contains 123 α-helices and 191 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: 20 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	13-18	6	1
α-helix	22-32	11
β-strand	38-41	4	1
α-helix	45-47	3
α-helix	58-62	5
α-helix	64-85	22
β-strand	88	1	2
β-strand	96	1	3
α-helix	98-122	25
β-strand	126-128	3	1
β-strand	131-136	6	4
β-strand	139-143	5	4
β-strand	149-153	5	4
β-strand	154-159	6	1
β-strand	163-165	3	5
α-helix	173-176	4
β-strand	178	1	6
α-helix	180-183	4
β-strand	193-196	4	6
α-helix	200-211	12
β-strand	216-220	5	6
α-helix	230-242	13
β-strand	246-249	4	6
β-strand	251-260	10	7
β-strand	266-273	8	7
β-strand	279-284	6	7
β-strand	286-289	4	6
β-strand	293-295	3	5
α-helix	303-305	3
β-strand	316	1	8
β-strand	323	1	1
β-strand	329-331	3	1
β-strand	336	1	8
α-helix	343-359	17
α-helix	363-365	3
β-strand	372-374	3	9
β-strand	380-384	5	9
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	9
α-helix	409-411	3
β-strand	421-428	8	9
α-helix	429-431	3
β-strand	434-441	8	9
α-helix	445-456	12
β-strand	461	1	9
α-helix	462-466	5
α-helix	469-471	3
α-helix	476-481	6
β-strand	485	1	9

Chain B: 20 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	13-18	6	10
α-helix	22-33	12
β-strand	38-41	4	10
α-helix	45-47	3
α-helix	58-62	5
α-helix	64-85	22
β-strand	88	1	3
β-strand	96	1	2
α-helix	98-121	24
β-strand	125-128	4	10
β-strand	131-136	6	11
β-strand	139-143	5	11
β-strand	149-153	5	11
β-strand	154-159	6	10
β-strand	163-165	3	12
α-helix	173-176	4
β-strand	178	1	13
α-helix	180-183	4
β-strand	193-196	4	13
α-helix	200-211	12
β-strand	216-220	5	13
β-strand	226	1	14
β-strand	228	1	14
α-helix	230-242	13
β-strand	246-249	4	13
β-strand	251-260	10	15
β-strand	266-273	8	15
β-strand	279-284	6	15
β-strand	286-289	4	13
β-strand	293-295	3	12
α-helix	303-305	3
β-strand	316	1	16
β-strand	323	1	10
β-strand	329-331	3	10
β-strand	336	1	16
α-helix	343-359	17
β-strand	372-374	3	17
β-strand	380-384	5	17
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	17
α-helix	409-411	3
β-strand	421-428	8	17
α-helix	429-431	3
β-strand	434-441	8	17
α-helix	445-456	12
β-strand	461	1	17
α-helix	462-467	6
α-helix	469-471	3
α-helix	475-480	6
β-strand	485	1	17
α-helix	486-488	3

Chain C: 22 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	13-18	6	18
α-helix	22-32	11
β-strand	38-41	4	18
α-helix	45-47	3
α-helix	57-62	6
α-helix	64-86	23
β-strand	88	1	19
β-strand	95-96	2	20
α-helix	98-122	25
β-strand	126-128	3	18
β-strand	131-136	6	21
β-strand	139-143	5	21
β-strand	149-153	5	21
β-strand	154-159	6	18
β-strand	163-165	3	22
α-helix	173-176	4
β-strand	178	1	23
α-helix	180-183	4
β-strand	193-196	4	23
α-helix	200-211	12
β-strand	216-220	5	23
β-strand	226	1	24
β-strand	228	1	24
α-helix	230-242	13
β-strand	246-249	4	23
β-strand	251-257	7	25
β-strand	267-273	7	25
β-strand	279-284	6	25
β-strand	286-288	3	23
β-strand	293-295	3	22
α-helix	303-305	3
α-helix	315	1
β-strand	316	1	26
α-helix	317	1
β-strand	323	1	18
β-strand	329-331	3	18
β-strand	336	1	26
α-helix	343-359	17
α-helix	363-365	3
β-strand	372-374	3	27
β-strand	380-384	5	27
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	27
α-helix	409-411	3
β-strand	421-428	8	27
α-helix	429-431	3
β-strand	434-441	8	27
α-helix	445-457	13
β-strand	461	1	27
α-helix	462-467	6
α-helix	469-471	3
α-helix	475-480	6
β-strand	485	1	27

Chain D: 21 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	13-18	6	28
α-helix	22-31	10
α-helix	32-34	3
β-strand	38-41	4	28
α-helix	45-47	3
α-helix	58-62	5
α-helix	64-87	24
β-strand	88-89	2	20
β-strand	96	1	19
α-helix	98-122	25
β-strand	126-128	3	28
β-strand	131-136	6	29
β-strand	139-143	5	29
β-strand	149-153	5	29
β-strand	154-159	6	28
β-strand	163-165	3	30
α-helix	173-176	4
β-strand	178	1	31
α-helix	180-183	4
β-strand	193-196	4	31
α-helix	200-211	12
β-strand	216-220	5	31
β-strand	226	1	32
β-strand	228	1	32
α-helix	230-242	13
β-strand	246-249	4	31
β-strand	251-260	10	33
β-strand	266-273	8	33
β-strand	279-284	6	33
β-strand	286-289	4	31
β-strand	293-295	3	30
α-helix	303-305	3
β-strand	316	1	34
β-strand	323	1	28
β-strand	329-331	3	28
β-strand	336	1	34
α-helix	343-359	17
α-helix	363-365	3
β-strand	372-374	3	35
β-strand	380-384	5	35
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	35
α-helix	409-412	4
β-strand	421-428	8	35
α-helix	429-431	3
β-strand	434-441	8	35
α-helix	445-456	12
β-strand	461	1	35
α-helix	462-467	6
α-helix	469-471	3
α-helix	475-480	6
β-strand	485	1	35

Chain E: 20 helices, 31 β-strands

Element	Residues	Length	Sheet
β-strand	13-18	6	36
α-helix	22-33	12
β-strand	38-41	4	36
α-helix	45-47	3
α-helix	58-61	4
α-helix	64-86	23
β-strand	88	1	37
β-strand	96	1	38
α-helix	98-121	24
β-strand	126-128	3	36
β-strand	131-136	6	39
β-strand	139-143	5	39
β-strand	149-153	5	39
β-strand	154-159	6	36
β-strand	165	1	40
α-helix	173-176	4
β-strand	178	1	41
α-helix	180-183	4
β-strand	193-196	4	41
α-helix	200-211	12
β-strand	216-220	5	41
α-helix	230-242	13
β-strand	246-249	4	41
β-strand	251-258	8	42
β-strand	267-273	7	42
β-strand	279-280	2	42
β-strand	283-284	2	42
β-strand	286-289	4	41
β-strand	293	1	40
α-helix	303-305	3
β-strand	316	1	43
β-strand	323	1	36
β-strand	329-331	3	36
β-strand	336	1	43
α-helix	343-359	17
α-helix	363-365	3
β-strand	372-374	3	44
β-strand	380-384	5	44
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	44
α-helix	409-411	3
β-strand	421-428	8	44
α-helix	429-431	3
β-strand	434-441	8	44
α-helix	445-456	12
β-strand	461	1	44
α-helix	462-467	6
α-helix	469-471	3
α-helix	475-480	6
β-strand	485	1	44

Chain F: 20 helices, 34 β-strands

Element	Residues	Length	Sheet
β-strand	13	1	45
β-strand	15-18	4	46
α-helix	22-32	11
β-strand	38-41	4	46
α-helix	45-47	3
α-helix	57-62	6
α-helix	64-85	22
β-strand	88	1	38
β-strand	96	1	37
α-helix	98-122	25
β-strand	126-128	3	46
β-strand	131-136	6	47
β-strand	139-143	5	47
β-strand	149-153	5	47
β-strand	154	1	45
β-strand	157-159	3	46
β-strand	163-165	3	48
α-helix	166-167	2
α-helix	173-176	4
β-strand	178	1	49
α-helix	180-183	4
β-strand	193-196	4	49
α-helix	200-211	12
β-strand	216-220	5	49
β-strand	226	1	50
β-strand	228	1	50
α-helix	230-242	13
β-strand	246-249	4	49
β-strand	251-260	10	51
β-strand	266-273	8	51
β-strand	280-284	5	51
β-strand	286-289	4	49
β-strand	293-295	3	48
α-helix	303-305	3
β-strand	316	1	52
β-strand	323	1	46
β-strand	329-331	3	46
β-strand	336	1	52
α-helix	343-359	17
α-helix	363-365	3
β-strand	372-374	3	53
β-strand	380-384	5	53
α-helix	387-394	8
β-strand	399-406	8	53
α-helix	409-412	4
β-strand	421-428	8	53
α-helix	429-431	3
β-strand	434-441	8	53
α-helix	445-456	12
β-strand	461	1	53
α-helix	462-467	6
α-helix	469-471	3
α-helix	476-478	3
β-strand	485	1	53

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Thioredoxin reductase 1	A, B, C, D, E, F	protein	519	HOMO SAPIENS	Q16881

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

>2J3N_1 THIOREDOXIN REDUCTASE 1 (chains A, B, C, D, E, F)
MGSSHHHHHHSSGLVPRGSHMNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMV
LDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDR
MIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIA
TGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMV
RSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLRVVAQSTNSEEII
EGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDKV
ELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIE
VYHSYFWPLEWTIPSRDNNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGL
TKKQLDSTIGIHPVCAEVFTTLSVTKRSGASILQAGCCG

Ligands and cofactors

ID	Name	Formula	Copies
FAD	Flavin-adenine dinucleotide	C27 H33 N9 O15 P2	6
NAP	NADP nicotinamide-adenine-dinucleotide phosphate	C21 H28 N7 O17 P3	6

Water and common crystallization additives (MPD) are not listed.

Primary citation

The Structure of Human Thioredoxin Reductase 1 Provides Insights Into C-Terminal Rearrangements During Catalysis. Fritz-Wolf, K., Urig, S., Becker, K. J Mol Biol (2007) 370:116. DOI 10.1016/J.JMB.2007.04.044 · PubMed

Other PDB entries of the same protein (UniProt Q16881), best resolution first:

3QFA 2.2 Å, Crystal structure of the human thioredoxin reductase-thioredoxin complex
2ZZC 2.6 Å, Crystal structure of NADP(H):human thioredoxin reductase I
3QFB 2.6 Å, Crystal structure of the human thioredoxin reductase-thioredoxin complex
2CFY 2.7 Å, Crystal structure of human thioredoxin reductase 1
2ZZ0 2.8 Å, Crystal structure of human thioredoxin reductase I (SeCys 498 Cys)
9UIN 3.03 Å, Human thioredoxin reductase 1 (SeCys 498 Cys) with Cu(I)
2ZZB 3.2 Å, Crystal structure of human thioredoxin reductase I and terpyridine platinum(II)
7X1R 3.9 Å, Cryo-EM structure of human thioredoxin reductase bound by Au

Browse structure collections

About this viewer

MolViewer shows 2J3N directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.