1BRO: Bromoperoxidase A2

Bromoperoxidase A2. Determined by X-ray diffraction at 2.05 Å resolution. Released 7 Dec 1996.

Method: X-ray diffraction
Resolution: 2.05 Å
Organism: Streptomyces aureofaciens
Chains: 2
Atoms: 4,529
Mol. weight: 60.56 kDa
Released: 7 Dec 1996

Explore 1BRO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1BRO contains 30 α-helices and 28 β-strands across 2 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: 14 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	2-8	7	1
β-strand	11-16	6	1
β-strand	17-20	4	2
β-strand	25-29	5	2
α-helix	36-39	4
α-helix	40-48	9
β-strand	52-56	5	2
α-helix	57-58	2
α-helix	73-87	15
β-strand	92-97	6	2
α-helix	99-111	13
β-strand	116-122	7	2
β-strand	130	1	3
β-strand	140	1	3
α-helix	142-154	13
α-helix	156-168	13
α-helix	170-173	4
β-strand	174	1	4
β-strand	178	1	4
α-helix	180-191	12
α-helix	195-204	10
α-helix	213-215	3
β-strand	220-225	6	2
α-helix	237-243	7
β-strand	248-252	5	2
α-helix	259-262	4
α-helix	264-276	13

Chain B: 16 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	2-8	7	5
β-strand	11-16	6	5
β-strand	17-20	4	6
β-strand	25-29	5	6
α-helix	36-39	4
α-helix	40-48	9
β-strand	52-56	5	6
α-helix	57-58	2
α-helix	73-87	15
β-strand	92-97	6	6
α-helix	99-111	13
β-strand	116-122	7	6
β-strand	128	1	7
β-strand	130	1	8
β-strand	140	1	8
α-helix	142-154	13
α-helix	156-167	12
α-helix	170-173	4
β-strand	174	1	9
β-strand	178	1	9
α-helix	180-191	12
α-helix	195-200	6
α-helix	201-204	4
β-strand	208	1	7
α-helix	213-215	3
β-strand	220-225	6	6
α-helix	233-235	3
α-helix	237-243	7
β-strand	248-252	5	6
α-helix	259-262	4
α-helix	264-276	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bromoperoxidase A2	A, B	protein	277	Streptomyces aureofaciens	P29715 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1BRO_1 BROMOPEROXIDASE A2 (chains A, B)
PFITVGQENSTSIDLYYEDHGTGQPVVLIHGFPLSGHSWERQSAALLDAGYRVITYDRRG
FGQSSQPTTGYDYDTFAADLNTVLETLDLQDAVLVGFSMGTGEVARYVSSYGTARIAKVA
FLASLEPFLLKTDDNPDGAAPQEFFDGIVAAVKADRYAFYTGFFNDFYNLDENLGTRISE
EAVRNSWNTAASGGFFAAAAAPTTWYTDFRADIPRIDVPALILHGTGDRTLPIENTARVF
HKALPSAEYVEVEGAPHGLLWTHAEEVNTALLAFLAK

Primary citation

The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold. Hecht, H.J., Sobek, H., Haag, T. et al. Nat Struct Biol (1994) 1:532-537. DOI 10.1038/nsb0894-532 · PubMed

Other PDB entries of the same protein (UniProt P29715 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1BRT 1.5 Å, Bromoperoxidase A2 mutant M99T
3VDX 3.0 Å, Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains
4IQ4 3.5 Å, Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains,…
4ITV 3.6 Å, Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains,…
4D9J 3.92 Å, Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains
4QES 4.19 Å, Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains,…
4QF0 6.49 Å, Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains,…
4IVJ 7.35 Å, Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains,…
4QFF 7.81 Å, Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains,…

Browse structure collections

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