2ZZ0: Human thioredoxin reductase I

Crystal structure of human thioredoxin reductase I (SeCys 498 Cys). Determined by X-ray diffraction at 2.8 Å resolution. Released 18 Aug 2009.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 15,818
Mol. weight: 229.49 kDa
Ligands: FAD
Released: 18 Aug 2009

Explore 2ZZ0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2ZZ0 contains 78 α-helices and 128 β-strands across 4 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, 32 β-strands

Element	Residues	Length	Sheet
β-strand	13	1	1
β-strand	15-18	4	2
α-helix	22-33	12
β-strand	38-41	4	2
α-helix	45-47	3
α-helix	58-62	5
α-helix	64-85	22
β-strand	88	1	3
β-strand	96	1	4
α-helix	98-122	25
β-strand	126-128	3	2
β-strand	131-136	6	5
β-strand	139-143	5	5
β-strand	149-153	5	5
β-strand	154	1	1
β-strand	157-159	3	2
β-strand	163-165	3	6
α-helix	173-176	4
β-strand	178-179	2	7
α-helix	180-183	4
β-strand	193-196	4	7
α-helix	200-211	12
β-strand	216-220	5	7
α-helix	230-242	13
β-strand	246-249	4	7
β-strand	251-260	10	8
β-strand	266-273	8	8
β-strand	279-284	6	8
β-strand	286-289	4	7
β-strand	293-295	3	6
α-helix	302-305	4
β-strand	316	1	9
β-strand	323	1	2
β-strand	329-331	3	2
β-strand	336	1	9
α-helix	343-359	17
β-strand	372-374	3	10
β-strand	380-384	5	10
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	10
α-helix	409-411	3
β-strand	421-428	8	10
α-helix	429-431	3
β-strand	434-441	8	10
α-helix	445-456	12
β-strand	461	1	10
α-helix	462-466	5
α-helix	469-471	3
α-helix	475-479	5
β-strand	485	1	10

Chain B: 20 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	13	1	11
β-strand	15-18	4	12
α-helix	22-33	12
β-strand	38-41	4	12
α-helix	45-47	3
α-helix	58-61	4
α-helix	64-85	22
β-strand	88	1	4
β-strand	96	1	3
α-helix	98-122	25
β-strand	126-128	3	12
β-strand	131-136	6	13
β-strand	139-143	5	13
β-strand	149-153	5	13
β-strand	154	1	11
β-strand	157-159	3	12
β-strand	163-165	3	14
α-helix	173-176	4
β-strand	178-179	2	15
α-helix	180-183	4
β-strand	193-196	4	15
α-helix	200-211	12
β-strand	216-220	5	15
α-helix	230-242	13
β-strand	246-249	4	15
β-strand	251-260	10	16
β-strand	266-273	8	16
β-strand	279-284	6	16
β-strand	286-289	4	15
β-strand	293-295	3	14
α-helix	302-305	4
β-strand	316	1	17
β-strand	323	1	12
β-strand	329-331	3	12
β-strand	336	1	17
α-helix	343-358	16
α-helix	363-365	3
β-strand	372-374	3	18
β-strand	380-384	5	18
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	18
α-helix	409-412	4
β-strand	421-428	8	18
α-helix	429-431	3
β-strand	434-441	8	18
α-helix	445-456	12
β-strand	461	1	18
α-helix	462-466	5
α-helix	469-470	2
α-helix	475-480	6
β-strand	485	1	18

Chain C: 19 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	13	1	19
β-strand	15-18	4	20
α-helix	22-33	12
β-strand	38-41	4	20
α-helix	58-62	5
α-helix	64-85	22
β-strand	88	1	21
β-strand	96	1	22
α-helix	98-122	25
β-strand	126-128	3	20
β-strand	131-136	6	23
β-strand	139-143	5	23
β-strand	149-153	5	23
β-strand	154	1	19
β-strand	157-159	3	20
β-strand	163-165	3	24
α-helix	173-176	4
β-strand	178-179	2	25
α-helix	180-183	4
β-strand	193-196	4	25
α-helix	200-211	12
β-strand	216-220	5	25
α-helix	230-242	13
β-strand	246-249	4	25
β-strand	251-260	10	26
β-strand	266-273	8	26
β-strand	279-284	6	26
β-strand	286-289	4	25
β-strand	293-295	3	24
α-helix	303-305	3
β-strand	316	1	27
β-strand	323	1	20
β-strand	329-331	3	20
β-strand	336	1	27
α-helix	343-359	17
α-helix	363-365	3
β-strand	372-374	3	28
β-strand	380-384	5	28
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	28
α-helix	409-412	4
β-strand	421-428	8	28
α-helix	429-431	3
β-strand	434-441	8	28
α-helix	445-457	13
β-strand	461	1	28
α-helix	462-466	5
α-helix	469-470	2
α-helix	475-479	5
β-strand	485	1	28

Chain D: 20 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	13	1	29
β-strand	15-18	4	30
α-helix	22-32	11
β-strand	38-41	4	30
α-helix	45-47	3
α-helix	58-62	5
α-helix	64-85	22
β-strand	88	1	22
β-strand	96	1	21
α-helix	98-122	25
β-strand	126-128	3	30
β-strand	131-136	6	31
β-strand	139-143	5	31
β-strand	149-153	5	31
β-strand	154	1	29
β-strand	157-159	3	30
β-strand	163-165	3	32
α-helix	173-176	4
β-strand	178-179	2	33
α-helix	180-183	4
β-strand	193-196	4	33
α-helix	200-211	12
β-strand	216-219	4	33
α-helix	230-242	13
β-strand	246-248	3	33
β-strand	251-260	10	34
β-strand	266-273	8	34
β-strand	279-284	6	34
β-strand	286-289	4	33
β-strand	293-295	3	32
α-helix	302-305	4
β-strand	316	1	35
β-strand	323	1	30
β-strand	329-331	3	30
β-strand	336	1	35
α-helix	343-359	17
α-helix	363-365	3
β-strand	372-374	3	36
β-strand	380-384	5	36
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	36
α-helix	409-412	4
β-strand	421-428	8	36
α-helix	429-431	3
β-strand	434-441	8	36
α-helix	445-456	12
β-strand	461	1	36
α-helix	462-466	5
α-helix	469-470	2
α-helix	475-480	6
β-strand	485	1	36

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Thioredoxin reductase 1, cytoplasmic	A, B, C, D	protein	513	Homo sapiens	Q16881

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

>2ZZ0_1 Thioredoxin reductase 1, cytoplasmic (chains A, B, C, D)
MAHHHHHHVDDDDKMNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTP
TPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQ
NHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPR
YLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLR
GFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLRVVAQSTNSEEIIEGEYNT
VMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVA
IQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYF
WPLEWTIPSRDNNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLD
STIGIHPVCAEVFTTLSVTKRSGASILQAGCCG

Ligands and cofactors

ID	Name	Formula	Copies
FAD	Flavin-adenine dinucleotide	C27 H33 N9 O15 P2	4

Water and common crystallization additives (SO4) are not listed.

Primary citation

Terpyridine-platinum(II) complexes are effective inhibitors of mammalian topoisomerases and human thioredoxin reductase 1. Lo, Y.C., Ko, T.P., Su, W.C. et al. J Inorg Biochem (2009) 103:1082-1092. DOI 10.1016/j.jinorgbio.2009.05.006 · 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
2J3N 2.8 Å, X-ray structure of human thioredoxin reductase 1
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

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