Structure of PDB 1g8k Chain E

Receptor sequence

>1g8kE (length=822) Species: 511 (Alcaligenes faecalis)

NDRITLPPANAQRTNMTCHFCIVGCGYHVYKWPELEEGGRAPEQNALGLD
FRKQLPPLAVTLTPAMTNVVTEHDGARYDIMVVPDKACVVNSGLSSTRGG
KMASYMYTPTGDGKERLSAPRLYAADEWVDTTWDHAMALYAGLIKKTLDK
DGPQGVFFSCFDHGGAGGGFENTWGTGKLMFSAIQTPMVRIHNRPAYNSE
CHATREMGIGELNNAYEDAQLADVIWSIGNNPYESQTNYFLNHWLPNLQG
ATTSKKKERFPNENFPQARIIFVDPRETPSVAIARHVAGNDRVLHLAIEP
GTDTALFNGLFTYVVEQGWIDKPFIEAHTKGFDDAVKTNRLSLDECSNIT
GVPVDMLKRAAEWSYKPKASGQAPRTMHAYEKGIIWGNDNYVIQSALLDL
VIATHNVGRRGTGCVRMGGHQEGYTRPPYPGDKKIYIDQELIKGKGRIMT
WWGCNNFQTSNNAQALREAILQRSAIVKQAMQKARGATTEEMVDVIYEAT
QNGGLFVTSINLYPTKLAEAAHLMLPAAHPGEMNLTSMNGERRIRLSEKF
MDPPGTAMADCLIAARIANALRDMYQKDGKAEMAAQFEGFDWKTEEDAFN
DGFRRAGQPGAPAIDSQGGSTGHLVTYDRLRKSGNNGVQLPVVSWDESKG
LVGTEMLYTEGKFDTDDGKAHFKPAPWNGLPATVQQQKDKYRFWLNNGRN
NEVWQTAYHDQYNSLMQERYPMAYIEMNPDDCKQLDVTGGDIVEVYNDFG
STFAMVYPVAEIKRGQTFMLFGYVNGIQGDVTTDWTDRDIIPYYKGTWGD
IRKVGSMSEFKRTVSFKSRRFG

3D structure

• PDB: 1g8k Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A.
• Chain: E
• Resolution: 1.64 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C24 S98 S99 R101 A199 Y200 S238 G421
• Catalytic site (residue number reindexed from 1): C21 S95 S96 R98 A196 Y197 S235 G418
• Enzyme Commision number: 1.20.9.1: arsenate reductase (azurin).

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	CA	E	Q467 S754 D783	Q464 S751 D780
BS02	MGD	E	G170 H195 N196 W389 H423 G456 C457 N458 T462 I513 N514 L515 A530 D563 N700 R702 Q708 T709 Y711 F774 Y797	G167 H192 N193 W386 H420 G453 C454 N455 T459 I510 N511 L512 A527 D560 N697 R699 Q705 T706 Y708 F771 Y794
BS03	MGD	E	R101 G232 N233 E237 S238 V276 D277 P278 R279 G304 D306 E384 K385 G386 G422 H423 W697 N699 G701 R702 N703 N704 V706 W707 Q708 K798	R98 G229 N230 E234 S235 V273 D274 P275 R276 G301 D303 E381 K382 G383 G419 H420 W694 N696 G698 R699 N700 N701 V703 W704 Q705 K795
BS04	F3S	E	C21 C24 V26 G27 C28 Y30 S99 R101 G102 N241	C18 C21 V23 G24 C25 Y27 S96 R98 G99 N238

Gene Ontology

Molecular Function

• GO:0016491 oxidoreductase activity
• GO:0043546 molybdopterin cofactor binding
• GO:0046872 metal ion binding
• GO:0050611 arsenate reductase (azurin) activity
• GO:0051536 iron-sulfur cluster binding
• GO:0051538 3 iron, 4 sulfur cluster binding

Biological Process

• GO:0045333 cellular respiration

Cellular Component

• GO:1990204 oxidoreductase complex

External links

• PDB: RCSB:1g8k, PDBe:1g8k, PDBj:1g8k
• PDBsum: 1g8k
• PubMed: 11250197
• UniProt: Q7SIF4|AIOA_ALCFA Arsenite oxidase subunit AioA (Gene Name=aioA)