Structure of PDB 8brq Chain B

Receptor sequence
>8brqB (length=525) Species: 1679168 (Bacillus sp. FJAT-27231) [Search protein sequence]
SNAMIIGAKKSKSGNALLFSGPQVGFVAPGFLYEVGLHSPGFDMEGSGFI
GYPFIMFGANQHLALTATAGYGNVTDIFEEKLNPANSTQYFYKGKWRNME
KRTETFIVRGGKSKKIEETFFHTVHGPVISLDAAANVAYSKSWSFRGTEA
KSIQAYMKANWAKNVKEFQQAASEFTMSLNWYYADKKGNIAYYHVGKYPI
RSNQIDDRFPTPGTGEYEWKGFQSFAKNPQAINPKKGYVVNWNNKPSKYW
RNGEYSIVWGKDNRVQQFINGIEARGKVDLKDLNEINYTASFAQLRTHYF
KPLLIKTLEKYQSENKEYAYLVEQLRKWNNLKEDKNHDGYYDAGVAAFFD
EWWNNTHDKLFNDSLGIVSDLTREITDHRMGATLAYKVLSGEPTNYQWKS
AAAAEKIILESTDEALAKLHKEKGEEADKWRAPIKTMTFGAKSLIAIPHG
YGSKTEIIEMNRGSENHYIEMTPKQPEGFNVTPPGQIGFIHKDGTLSEHY
EDQLSLYANWKFKPFLFDKKDVKRA
3D structure
PDB8brq Multistep Engineering of a Penicillin G Acylase for Systematic Improvement of Crystallization Efficiency
ChainB
Resolution1.63 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 A67 S1 P22 A67
BS02 BU3 B G190 N191 G188 N189
BS03 CA B N73 T75 D76 E256 N73 T75 D76 E254
BS04 CA B D336 N338 D340 Y342 D344 D334 N336 D338 Y340 D342
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:8brq, PDBe:8brq, PDBj:8brq
PDBsum8brq
PubMed
UniProtA0A0K9H482

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