1SZG: Cytochrome b2, mitochondrial

A198G:L230A flavocytochrome b2 with sulfite bound. Determined by X-ray diffraction at 2.7 Å resolution. Released 27 Jul 2004.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 6,255
Mol. weight: 114.29 kDa
Ligands: FNS
Released: 27 Jul 2004

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

Secondary structure: helices and β-sheets

1SZG contains 47 α-helices and 29 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: 23 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	107-112	6
α-helix	117-118	2
α-helix	119-121	3
α-helix	125-135	11
α-helix	138-145	8
α-helix	152-159	8
α-helix	160-163	4
β-strand	165-166	2	1
β-strand	181-183	3	2
β-strand	186-188	3	2
β-strand	192-194	3	3
α-helix	209-217	9
β-strand	225-227	3	3
α-helix	228	1
α-helix	235-241	7
β-strand	249-253	5	3
α-helix	259-271	13
β-strand	277-280	4	3
α-helix	290-296	7
α-helix	332-339	8
β-strand	346-351	6	3
α-helix	354-362	9
β-strand	367-370	4	3
α-helix	373-375	3
α-helix	381-383	3
α-helix	384-397	14
β-strand	405-409	5	3
α-helix	415-424	10
β-strand	428-431	4	3
α-helix	433-465	33
α-helix	475-477	3
β-strand	478-479	2	1
β-strand	486-487	2	4
α-helix	489-492	4
α-helix	494-499	6
α-helix	505-509	5

Chain B: 24 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	105-115	11
α-helix	117-118	2
α-helix	119-121	3
α-helix	125-135	11
α-helix	138-145	8
α-helix	152-159	8
α-helix	160-163	4
β-strand	165-166	2	5
β-strand	178	1	6
β-strand	181-183	3	7
β-strand	186-188	3	7
β-strand	192-194	3	8
α-helix	200-202	3
α-helix	209-217	9
β-strand	225-227	3	8
α-helix	228	1
α-helix	235-239	5
β-strand	249-253	5	8
α-helix	259-272	14
β-strand	277-280	4	8
α-helix	290-296	7
α-helix	332-340	9
α-helix	345	1
β-strand	346-351	6	8
α-helix	354-362	9
β-strand	367-370	4	8
β-strand	381	1	1
α-helix	382-383	2
α-helix	384-396	13
β-strand	405-408	4	8
α-helix	415-424	10
β-strand	428-431	4	8
α-helix	433-465	33
β-strand	469	1	6
α-helix	470-472	3
α-helix	475-477	3
β-strand	478-479	2	5
β-strand	488-489	2	4
α-helix	490-492	3
α-helix	494-499	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytochrome b2, mitochondrial	A, B	protein	511	Saccharomyces cerevisiae	P00175 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1SZG_1 Cytochrome b2, mitochondrial (chains A, B)
EPKLDMNKQKISPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDVIKFNAGKDVTA
IFEPLHAPNVIDKYIAPEKKLGPLQGSMPPELVCPPYAPGETKEDIARKEQLKSLLPPLD
NIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDIS
TDMLGSHVDVPFYVSATGLCKLGNPLEGEKDVARGCGQGVTKVPQMISTAASCSPEEIIE
AAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQREKDMKLKFSNT
KAGPKAMKKTNVEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKA
AEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMPILEQRNLKDKLEVFVDGGVRRGTDVLK
ALCLGAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLLDL
STLKARTVGVPNDVLYNEVYEGPTLTEFEDA

Ligands and cofactors

ID	Name	Formula	Copies
FNS	N-sulfo-flavin mononucleotide	C17 H21 N4 O12 P S	2

Primary citation

Altered Substrate Specificity in Flavocytochrome b(2): Structural Insights into the Mechanism of l-Lactate Dehydrogenation. Mowat, C.G., Wehenkel, A., Green, A.J. et al. Biochemistry (2004) 43:9519-9526. DOI 10.1021/bi049263m · PubMed

Other PDB entries of the same protein (UniProt P00175 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1KBI 2.3 Å, Crystallographic Study of the Recombinant Flavin-binding Domain of Baker's Yeast…
1FCB 2.4 Å, Molecular structure of flavocytochrome B2 at 2.4 Å resolution
1KBJ 2.5 Å, Crystallographic Study of the Recombinant Flavin-binding Domain of Baker's Yeast…
1LTD 2.6 Å, The 2.6 Å refined structure of the escherichia coli recombinant saccharomyces cerevisiae…
1SZF 2.7 Å, A198G:L230A mutant flavocytochrome b2 with pyruvate bound
3KS0 2.7 Å, Crystal structure of the heme domain of flavocytochrome b2 in complex with Fab B2B4
1QCW 2.75 Å, Flavocytochrome B2, ARG289LYS mutant
2OZ0 2.8 Å, Mechanistic and Structural Studies of H373Q Flavocytochrome b2: Effects of Mutating the…
1LCO 2.9 Å, X-ray structure of two complexes of the Y143F flavocytochrome B2 mutant crystallized in…
1LDC 2.9 Å, X-ray structure of two complexes of the Y143F flavocytochrome B2 mutant crystallized in…
1SZE 3.0 Å, L230A mutant flavocytochrome b2 with benzoylformate
9J9B 3.83 Å, Substrate-engaged TIM23 complex from yeast

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