Structure of PDB 6nvw Chain B

Receptor sequence
>6nvwB (length=527) Species: 1404 (Priestia megaterium) [Search protein sequence]
SNAAIVGSEKSATGNALLFSGPQVGFVAPGFLYEVGLHAPGFDMEGSGFI
GYPFIMFGANNHFALSATAGYGNVTDIFEEKLNAKNSSQYLYKGKWRDME
KRKESFTVKGDNGEKKTVEKIYYRTVHGPVISRDETNKVAYSKSWSFRGT
EAQSMSAYMKANWAKNLKEFENAASEYTMSLNWYYADKKGDIAYYHVGRY
PVRNSKIDERIPTPGTGEYEWKGFIPFKENPHVINPKNGYVVNWNNKPSK
EWVNGEYSFYWGEDNRVQQYINGMEARGKVTLEDINEINYTASFAQLRAN
LFKQLLIDVLDKNKSTNGNYIYLIEKLEEWNNLKEDENKDGYYDAGIAAF
FDEWWNNLHDKLFMDELGDFYGITKEITDHRYGASLAYKILNKESTNYKW
VNVDQEKIIMESTNEVLAKLQSEKGLKAEKWRMPIKTMTFGEKSLIGIPH
GYGSMTPIIEMNRGSENHYIEMTPTGPSGFNITPPGQIGFVKKDGTISDH
YDDQLVMFAEWKFKPYLFNKKDINKAA
3D structure
PDB6nvw Crystal structures and protein engineering of three different penicillin G acylases from Gram-positive bacteria with different thermostability.
ChainB
Resolution2.203 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S1 Q23 A69 N245 N467
Catalytic site (residue number reindexed from 1) S1 Q23 A69 N245 N467
Enzyme Commision number 3.5.1.11: penicillin amidase.
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 B N73 T75 D76 E256 N73 T75 D76 E256
BS02 CA B D336 N338 D340 Y342 Y343 D344 D336 N338 D340 Y342 Y343 D344
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
Biological Process
GO:0017000 antibiotic biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6nvw, PDBe:6nvw, PDBj:6nvw
PDBsum6nvw
PubMed31227867
UniProtQ60136|PAC_PRIMG Penicillin G acylase (Gene Name=pac)

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