Structure of PDB 4g39 Chain A

Receptor sequence

>4g39A (length=465) Species: 83333 (Escherichia coli K-12) [Search protein sequence]

MLLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILKKN
VKPVHQMLHSVGLDALATANDMNSNVLCTSNPYESQLHAEAYEWAKKISE
HLLPTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGG
GLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNA
KTKYTLERVGVETFKAEVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDN
WHLTLFIENGRILDYPARPLKTGLLEIAKIHKGDFRITANQNLIIAGVPE
SEKAKIEKIAKESGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFI
DNIDNLMAKHGVSDEHIVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHL
GGNRIGTRIPRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRA
GIIRPVLDPARDLWD

3D structure

PDB

4g39 Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer.

Chain

Resolution

2.4 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	R83 S153 K215 K217 A394 C434 C440 C479 C483
Catalytic site (residue number reindexed from 1)	R4 S74 K110 K112 A289 C329 C335 C374 C378
Enzyme Commision number	1.8.1.2: assimilatory sulfite reductase (NADPH).

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)	Binding affinity
BS01	SF4	A	C434 S436 C440 A443 G478 C479 N481 C483	C329 S331 C335 A338 G373 C374 N376 C378
BS02	SRM	A	R83 R113 T115 N116 R117 R214 K215 K217 S258 Q396 C434 V435 T439 C440 L442 N481 G482 C483 R485	R4 R34 T36 N37 R38 R109 K110 K112 S153 Q291 C329 V330 T334 C335 L337 N376 G377 C378 R380

Gene Ontology

	Molecular Function
GO:0004783	sulfite reductase (NADPH) activity
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:0050661	NADP binding
GO:0051536	iron-sulfur cluster binding
GO:0051539	4 iron, 4 sulfur cluster binding

	Biological Process
GO:0000103	sulfate assimilation
GO:0008652	amino acid biosynthetic process
GO:0019344	cysteine biosynthetic process
GO:0070814	hydrogen sulfide biosynthetic process

	Cellular Component
GO:0009337	sulfite reductase complex (NADPH)

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:4g39, PDBe:4g39, PDBj:4g39
PDBsum	4g39
PubMed	23153334
UniProt	P17846\|CYSI_ECOLI Sulfite reductase [NADPH] hemoprotein beta-component (Gene Name=cysI)

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