2ZZC: NADP(H):human thioredoxin reductase I

Crystal structure of NADP(H):human thioredoxin reductase I. Determined by X-ray diffraction at 2.6 Å resolution. Released 18 Aug 2009.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 16,283
Mol. weight: 232.08 kDa
Ligands: NAP, FAD
Released: 18 Aug 2009

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

Secondary structure: helices and β-sheets

2ZZC contains 85 α-helices and 120 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: 23 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	13-18	6	1
α-helix	22-33	12
β-strand	38-41	4	1
α-helix	45-47	3
α-helix	58-62	5
α-helix	64-83	20
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	302-304	3
α-helix	315	1
β-strand	316	1	8
α-helix	317	1
β-strand	323	1	1
β-strand	329-331	3	1
α-helix	333-335	3
β-strand	336	1	8
α-helix	343-358	16
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	409-412	4
β-strand	421-428	8	9
α-helix	429-431	3
β-strand	434-441	8	9
α-helix	445-457	13
β-strand	461	1	9
α-helix	462-466	5
α-helix	469-471	3
α-helix	475-479	5
β-strand	485	1	9

Chain B: 22 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	13-18	6	10
α-helix	22-32	11
β-strand	38-41	4	10
α-helix	45-47	3
α-helix	57-62	6
α-helix	64-85	22
β-strand	88	1	3
β-strand	96	1	2
α-helix	98-122	25
β-strand	126-128	3	10
β-strand	130-136	7	11
β-strand	139-144	6	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
α-helix	230-242	13
β-strand	246-249	4	13
β-strand	251-260	10	14
β-strand	266-273	8	14
β-strand	279-284	6	14
β-strand	286-289	4	13
β-strand	293-295	3	12
α-helix	302-305	4
α-helix	315	1
β-strand	316	1	15
α-helix	317	1
β-strand	323	1	10
β-strand	329-331	3	10
α-helix	333-335	3
β-strand	336	1	15
α-helix	343-358	16
β-strand	372-374	3	16
β-strand	380-384	5	16
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	16
α-helix	409-412	4
β-strand	421-428	8	16
α-helix	429-431	3
β-strand	434-441	8	16
α-helix	445-456	12
β-strand	461	1	16
α-helix	462-466	5
α-helix	469-470	2
α-helix	475-480	6
β-strand	485	1	16

Chain C: 18 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	13-18	6	17
α-helix	22-33	12
β-strand	38-41	4	17
α-helix	45-47	3
α-helix	57-62	6
α-helix	64-83	20
β-strand	88	1	18
β-strand	96	1	19
α-helix	98-122	25
β-strand	125-128	4	17
β-strand	130-136	7	20
β-strand	139-144	6	20
β-strand	149-153	5	20
β-strand	154-159	6	17
β-strand	163-165	3	21
α-helix	173-176	4
β-strand	178	1	22
α-helix	180-183	4
β-strand	193-196	4	22
α-helix	200-211	12
β-strand	216-220	5	22
α-helix	230-242	13
β-strand	246-249	4	22
β-strand	251-260	10	23
β-strand	266-273	8	23
β-strand	279-284	6	23
β-strand	286-289	4	22
β-strand	293-295	3	21
β-strand	316	1	24
β-strand	323	1	17
β-strand	329-331	3	17
β-strand	336	1	24
α-helix	343-358	16
α-helix	363-365	3
β-strand	371-374	4	25
β-strand	380-384	5	25
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	25
α-helix	409-412	4
β-strand	421-428	8	25
β-strand	434-441	8	25
α-helix	445-457	13
β-strand	461	1	25
α-helix	462-466	5
α-helix	469-470	2
α-helix	475-479	5
β-strand	485	1	25

Chain D: 22 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	13-18	6	26
α-helix	22-32	11
β-strand	38-41	4	26
α-helix	45-47	3
α-helix	58-62	5
α-helix	64-85	22
β-strand	88	1	19
β-strand	96	1	18
α-helix	98-122	25
β-strand	126-128	3	26
β-strand	131-136	6	27
β-strand	139-143	5	27
β-strand	149-153	5	27
β-strand	154-159	6	26
β-strand	163-165	3	28
α-helix	173-176	4
β-strand	178	1	29
α-helix	180-183	4
β-strand	193-196	4	29
α-helix	200-211	12
β-strand	216-220	5	29
α-helix	230-241	12
β-strand	246-249	4	29
β-strand	251-260	10	30
β-strand	266-273	8	30
β-strand	279-284	6	30
β-strand	286-289	4	29
β-strand	293-295	3	28
α-helix	303-305	3
α-helix	315	1
β-strand	316	1	31
α-helix	317	1
β-strand	323	1	26
β-strand	329-331	3	26
α-helix	333-335	3
β-strand	336	1	31
α-helix	343-358	16
β-strand	372-374	3	32
β-strand	379-384	6	32
α-helix	387-394	8
α-helix	396-398	3
β-strand	399-406	8	32
α-helix	409-412	4
β-strand	421-428	8	32
α-helix	429-431	3
β-strand	434-442	9	32
α-helix	445-456	12
β-strand	461	1	32
α-helix	462-466	5
α-helix	469-470	2
α-helix	475-480	6
β-strand	485	1	32

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

>2ZZC_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
NAP	NADP nicotinamide-adenine-dinucleotide phosphate	C21 H28 N7 O17 P3	4
FAD	Flavin-adenine dinucleotide	C27 H33 N9 O15 P2	4

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
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
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 2ZZC 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.