Structure of PDB 4g38 Chain A Binding Site BS02

Receptor Information

>4g38 Chain A (length=449) Species: 83333 (Escherichia coli K-12)

LLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILPVHQ
MLHSVGLDALATAWDMNRNVLCTSNPYESQLHAEAYEWAKKISEHLLPKF
KTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGGGLSIEHGNKKT
YARTASEFGYLPLEHTLAVAEAVVTTQRDWGNNAKTKYTLERVGVETFKA
EVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDNWHLTLFIENGRILDYP
ARPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKESGLM
NAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGVSDEH
IVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKEN
ITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGIIRPVLDPARDLWD

Ligand information

• Ligand ID: SRM
• InChI: InChI=1S/C42H46N4O16.Fe/c1-41(17-39(59)60)23(5-9-35(51)52)29-14-27-21(11-37(55)56)19(3-7-33(47)48)25(43-27)13-26-20(4-8-34(49)50)22(12-38(57)58)28(44-26)15-31-42(2,18-40(61)62)24(6-10-36(53)54)30(46-31)16-32(41)45-29;/h13-16,23-24H,3-12,17-18H2,1-2H3,(H10,43,44,45,46,47,48,49,50,51,52,53,54,55,56,57,58,59,60,61,62);/q;+2/p-2/t23?,24-,41+,42+;/m1./s1
• InChIKey: DLKSSIHHLYNIKN-MWBYXLBFSA-L
• SMILES:
  OpenEye OEToolkits 2.0.7: C[C@@]1(C(C2=[N]3C1=Cc4c(c(c5n4[Fe]36N7C(=C5)C(=C(C7=CC8=[N]6C(=C2)[C@@](C8CCC(=O)O)(C)CC(=O)O)CC(=O)O)CCC(=O)O)CCC(=O)O)CC(=O)O)CCC(=O)O)CC(=O)O
  ACDLabs 10.04: O=C(O)CCC=6C7=Cc1c(c(c2n1[Fe]84N5C(=CC3=C(CCC(=O)O)C(C(=C2)N34)(C)CC(=O)O)C(C(=C5C=C(C=6CC(=O)O)N78)CCC(=O)O)(C)CC(=O)O)CC(=O)O)CCC(=O)O
  OpenEye OEToolkits 2.0.7: CC1(C(C2=[N]3C1=Cc4c(c(c5n4[Fe]36N7C(=C5)C(=C(C7=CC8=[N]6C(=C2)C(C8CCC(=O)O)(C)CC(=O)O)CC(=O)O)CCC(=O)O)CCC(=O)O)CC(=O)O)CCC(=O)O)CC(=O)O
  CACTVS 3.385: C[C@]1(CC(O)=O)[C@@H](CCC(O)=O)C2=NC1=CC3=NC(=Cc4n5[Fe][N@@]6C(=C2)C(=C(CCC(O)=O)C6=Cc5c(CCC(O)=O)c4CC(O)=O)CC(O)=O)[C@@](C)(CC(O)=O)[C@@H]3CCC(O)=O
  CACTVS 3.385: C[C]1(CC(O)=O)[CH](CCC(O)=O)C2=NC1=CC3=NC(=Cc4n5[Fe][N]6C(=C2)C(=C(CCC(O)=O)C6=Cc5c(CCC(O)=O)c4CC(O)=O)CC(O)=O)[C](C)(CC(O)=O)[CH]3CCC(O)=O
• Formula: C42 H44 Fe N4 O16
• Name: SIROHEME
• PDB chain: 4g38 Chain A Residue 604

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4g38 Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer.
• Resolution: 1.56 Å
• Binding residue (original residue number in PDB): R83 R113 T115 N116 R117 Q121 H123 K215 K217 G256 L257 S258 Q396 C434 V435 T439 C440 L442 N481 G482 C483 R485
• Binding residue (residue number reindexed from 1): R3 R33 T35 N36 R37 Q41 H43 K99 K101 G140 L141 S142 Q275 C313 V314 T318 C319 L321 N360 G361 C362 R364
• Annotation score: 1

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).

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)

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)