Structure of PDB 8brt Chain B

Receptor sequence
>8brtB (length=526) Species: 1679168 (Bacillus sp. FJAT-27231) [Search protein sequence]
SNAMIIGAKKSKSANALLFSGPQVGFVAPGFLYEVGLHSPGFDMEGSGFI
GYPFIMFGANQHLALTATAGYGNVTDIFEEKLNPANSTQYFYKGKWRNME
KRTETFIVRGDGKSKKIEETFFHTVHGPVISLDAAANVAYSKSWSFRGTE
AKSIQAYMKANWAKNVKEFQQAASEFTMSLNWYYADKKGNIAYYHVGKYP
IRSNQIDDRFPTPGTGEYEWKGFQSFAKNPQAINPKKGYVVNWNNKPSKY
WRNGEYSIVWGKDNRVQQFINGIEARGKVDLKDLNEINYTASFAQLRTHY
FKPLLIKTLEKYQSENKEYAYLVEQLRKWNNLKEDKNHDGYYDAGVAAFF
DEWWNNTHDKLFNDSLGIVSDLTREITDHRMGATLAYKVLSGEPTNYQWK
SAAAAEKIILESTDEALAKLHKEKGEEADKWRAPIKTMTFGAKSLIAIPH
GYGSKTEIIEMNRGSENHYIEMTPKQPEGFNVTPPGQIGFIHKDGTLSEH
YEDQLSLYANWKFKPFLFDKKDVKRA
3D structure
PDB8brt Multistep Engineering of a Penicillin G Acylase for Systematic Improvement of Crystallization Efficiency
ChainB
Resolution1.31 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 BU3 B S1 P22 F49 A67 S1 P22 F49 A67
BS02 BU3 B Y290 W512 Y289 W511
BS03 CA B D336 N338 D340 Y342 D344 D335 N337 D339 Y341 D343
BS04 CA B N73 T75 D76 E256 N73 T75 D76 E255
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
Biological Process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:8brt, PDBe:8brt, PDBj:8brt
PDBsum8brt
PubMed
UniProtA0A0K9H482

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