Structure of PDB 4g38 Chain A

Receptor sequence

>4g38A (length=449) Species: 83333 (Escherichia coli K-12) [Search protein sequence]

LLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILPVHQ
MLHSVGLDALATAWDMNRNVLCTSNPYESQLHAEAYEWAKKISEHLLPKF
KTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGGGLSIEHGNKKT
YARTASEFGYLPLEHTLAVAEAVVTTQRDWGNNAKTKYTLERVGVETFKA
EVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDNWHLTLFIENGRILDYP
ARPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKESGLM
NAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGVSDEH
IVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKEN
ITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGIIRPVLDPARDLWD

3D structure

PDB

4g38 Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer.

Chain

Resolution

1.56 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 R153 K215 K217 A394 C434 C440 C479 C483
Catalytic site (residue number reindexed from 1)	R3 R68 K99 K101 A273 C313 C319 C358 C362
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 L442 A443 G478 C479 N481 C483	C313 S315 C319 L321 A322 G357 C358 N360 C362
BS02	SRM	A	R83 R113 T115 N116 R117 Q121 H123 K215 K217 G256 L257 S258 Q396 C434 V435 T439 C440 L442 N481 G482 C483 R485	R3 R33 T35 N36 R37 Q41 H43 K99 K101 G140 L141 S142 Q275 C313 V314 T318 C319 L321 N360 G361 C362 R364

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:4g38, PDBe:4g38, PDBj:4g38
PDBsum	4g38
PubMed	23153334
UniProt	P17846\|CYSI_ECOLI Sulfite reductase [NADPH] hemoprotein beta-component (Gene Name=cysI)

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