Structure of PDB 1y54 Chain A

Receptor sequence
>1y54A (length=359) Species: 550 (Enterobacter cloacae) [Search protein sequence]
VSEKQLAEVVANTITPLMKAQSVPGMAVAVIYQGKPHYYTFGKADIAANK
PVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDPVTRYWPQLTGKQWQ
GIRMLDLATYTAGGLPLQVPDEVTDNASLVRFYQNWQPQWKPGTTRLYAN
ASIGLFGALAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAWG
YRDGKAVRVSPGMLDAQAYGVKTNVQDMANWVMANMAPENVADASLKQGI
ALAQSRYWRIGSMYQGLGWEMLNWPVEANTVVEGSDSKVALAPLPVVEVN
PPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLANTSYPNPARVEA
AYHILEALQ
3D structure
PDB1y54 Crystal Structure of BRL 42715, C6-(N1-Methyl-1,2,3-triazolylmethylene)penem, in Complex with Enterobactercloacae 908R beta-Lactamase: Evidence for a Stereoselective Mechanism from Docking Studies
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y112 V121 Y150 G156 E272 K315 S318
Catalytic site (residue number reindexed from 1) S62 K65 Y110 V119 Y148 G154 E270 K313 S316
Enzyme Commision number 3.5.2.6: beta-lactamase.
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 FDT A S64 Q120 N152 Y221 G317 S318 S62 Q118 N150 Y219 G315 S316
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1y54, PDBe:1y54, PDBj:1y54
PDBsum1y54
PubMed15755127
UniProtP05364|AMPC_ENTCL Beta-lactamase (Gene Name=ampC)

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