8GBK: Ssr1698 protein

Dri1 hemoprotein variant H79A-R90A with a zinc-mirror heme site. Determined by X-ray diffraction at 2.9 Å resolution. Released 24 Apr 2024.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Synechocystis sp. PCC 6803 substr. Kazusa
Chains: 8
Atoms: 5,920
Mol. weight: 91.7 kDa
Ligands: HEB
Released: 24 Apr 2024

Explore 8GBK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8GBK contains 33 α-helices and 40 β-strands across 8 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: 5 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	11
α-helix	7-20	14
α-helix	22-27	6
α-helix	28-32	5
β-strand	41-46	6	12
β-strand	50-56	7	12
β-strand	61-67	7	12
α-helix	71-72	2
β-strand	74	1	11
α-helix	75-95	21

Chain B: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	7
α-helix	7-20	14
α-helix	22-31	10
β-strand	40-46	7	6
β-strand	50-57	8	6
β-strand	60-67	8	6
α-helix	71-72	2
β-strand	74	1	7
α-helix	75-94	20
β-strand	98	1	5

Chain C: 4 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	13
α-helix	7-19	13
α-helix	22-31	10
β-strand	41-46	6	3
β-strand	50-55	6	3
β-strand	62-67	6	3
α-helix	71-72	2
β-strand	74	1	13
α-helix	75-93	19

Chain D: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
α-helix	22-31	10
β-strand	41-46	6	10
β-strand	50-55	6	10
β-strand	63-67	5	10
α-helix	71-72	2
α-helix	75-94	20

Chain E: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	8
α-helix	7-20	14
α-helix	22-31	10
β-strand	41-46	6	9
β-strand	50-56	7	9
β-strand	61-67	7	9
α-helix	71-72	2
β-strand	74	1	8
α-helix	75-94	20
β-strand	97-99	3	10

Chain F: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
α-helix	22-27	6
α-helix	28-32	5
β-strand	39-46	8	14
β-strand	50-56	7	14
β-strand	61-67	7	14
α-helix	71-72	2
α-helix	75-93	19

Chain G: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	1
α-helix	7-20	14
α-helix	22-31	10
β-strand	40-46	7	2
β-strand	50-56	7	2
β-strand	62-67	6	2
α-helix	71-72	2
β-strand	74	1	1
α-helix	75-94	20
β-strand	99-101	3	3

Chain H: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	4
α-helix	7-20	14
α-helix	22-31	10
β-strand	41-47	7	5
β-strand	50-55	6	5
β-strand	62-65	4	5
β-strand	74	1	4
α-helix	75-93	19
β-strand	97-99	3	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ssr1698 protein	A, B, C, D, E, F, G, H	protein	103	Synechocystis sp. PCC 6803 substr. Kazusa	P73129 (AlphaFold model)

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

>8GBK_1 Ssr1698 protein (chains A, B, C, D, E, F, G, H)
MADPLTPAISDRICKHMNEDHASAIALYAQVFGQQTDVTMAQMQAIDPTGMDLVVESEGG
SKTIRIEFEQPLKDSEDAAQVLIAMAKQAASVGKNSAENLYFQ

Ligands and cofactors

ID	Name	Formula	Copies
HEB	Heme b/c	C34 H34 Fe N4 O4	4

Primary citation

A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria. Grosjean, N., Yee, E.F., Kumaran, D. et al. Nat Commun (2024) 15:3167-3167. DOI 10.1038/s41467-024-47486-z · PubMed

Other PDB entries of the same protein (UniProt P73129 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8ZXQ 1.51 Å, Crystal structure of Ssr1698 in complex with heme b
8ZXR 1.6 Å, Crystal structure of Ssr1698 in complex with heme c
8GDW 2.35 Å, Crystal structure of Domain Related to Iron (DRI) from cyanobacteria
8FM6 2.85 Å, Dri1 hemoprotein variant H21A with a zinc-mirror heme site
8GF4 3.0 Å, Crystal structure of Domain Related to Iron (DRI) in complex with heme

Browse structure collections

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