Structure of PDB 5h92 Chain B

Receptor sequence

>5h92B (length=572) Species: 4577 (Zea mays) [Search protein sequence]

KRSKVEIIKEKSNFLRYPLNEELVSEAPNINESAVQLIKFHGSYQQTDRD
VRGQKNYSFMLRTKNPCGKVPNQLYLAMDTLADEFGIGTLRLTTRQTFQL
HGVLKKNLKTVLSTVIKNMGSTLGACGDLNRNVLAPAAPYVKKDILFAQQ
TAENIAALLTPQSGAYYDLWVDGEKIMSAEEPPEVTKARNDNSHGTNFPD
SPEPIYGTQYLPRKFKVAVTAAGDNSVDILTNDIGVVVVSDDAGEPIGFN
IYVGGGMGRTHRVETTFPRLADPLGYVPKEDILYAIKAIVVTQRENGRRD
DRKYSRMKYMIDRWGIDRFRAEVEKYYGKKFESFRPLPEWQFNSYLGWQE
QGDGKLFYGVHVDNGRVGGQAKKTLREIIEKYNLDVSITPNQNLILCGID
QAWREPITTALAQAGLLEPKDVDPLNLTAMACPALPLCPLAQTEAERGIL
PILKRIRAVFNKVGIKDSESVVVRITGCPNGCARPYMAELGFVGDGPKSY
QIWLGGTPNQSTLAESFMDKVKLDDIEKVLEPLFTYWNGTRQEGESFGSF
TNRTGFDKLKEVVNKWAESPSA

3D structure

PDB

5h92 Structural and mutational studies of an electron transfer complex of maize sulfite reductase and ferredoxin.

Chain

Resolution

2.08 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	R124 R193 K276 K278 P452 C494 C500 C540 C544 A634
Catalytic site (residue number reindexed from 1)	R62 R131 K214 K216 P390 C432 C438 C478 C482 A572
Enzyme Commision number	1.8.7.1: assimilatory sulfite reductase (ferredoxin).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)
BS01	SF4	B	C494 A496 C500 A503 T538 G539 C540 N542 C544	C432 A434 C438 A441 T476 G477 C478 N480 C482
BS02	SRM	B	Y106 Q108 R124 R153 T155 T156 R157 T159 Q161 H163 R275 K276 K278 G318 M319 G320 R368 Q454 P495 C500 P501 L502 N542 C544 R546	Y44 Q46 R62 R91 T93 T94 R95 T97 Q99 H101 R213 K214 K216 G256 M257 G258 R306 Q392 P433 C438 P439 L440 N480 C482 R484
BS03	MG	B	V424 N453 N455	V362 N391 N393

Gene Ontology

	Molecular Function
GO:0003677	DNA binding
GO:0003690	double-stranded DNA binding
GO:0016002	sulfite reductase activity
GO:0016491	oxidoreductase activity
GO:0020037	heme binding
GO:0046872	metal ion binding
GO:0050311	sulfite reductase (ferredoxin) activity
GO:0051536	iron-sulfur cluster binding
GO:0051539	4 iron, 4 sulfur cluster binding

	Biological Process
GO:0000103	sulfate assimilation
GO:0006790	sulfur compound metabolic process
GO:0009409	response to cold
GO:0019418	sulfide oxidation
GO:0045892	negative regulation of DNA-templated transcription
GO:1900160	plastid chromosome packaging

	Cellular Component
GO:0009337	sulfite reductase complex (NADPH)
GO:0009507	chloroplast
GO:0009570	chloroplast stroma
GO:0010319	stromule
GO:0042644	chloroplast nucleoid

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:5h92, PDBe:5h92, PDBj:5h92
PDBsum	5h92
PubMed	26920048
UniProt	O23813\|SIR_MAIZE Sulfite reductase [ferredoxin], chloroplastic (Gene Name=SIR)

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