Structure of PDB 1o07 Chain A

Receptor sequence
>1o07A (length=355) Species: 562 (Escherichia coli) [Search protein sequence]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLLVPDEVKSSSDLLRFYQNWQPAWAPGTQRLEANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSISDNKIALAARPVKAITPPTP
AVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQI
LNALQ
3D structure
PDB1o07 Structural Aspects for Evolution of beta-Lactamases from Penicillin-Binding Proteins
ChainA
Resolution1.71 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y112 A114 V121 E150 A151 G156 E272 K315 A318
Catalytic site (residue number reindexed from 1) S61 K64 Y109 A111 V118 E147 A148 G153 E269 K309 A312
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 MXG A S64 L119 E150 N152 R204 V211 S212 Y221 D288 A318 G320 N343 S61 L116 E147 N149 R201 V208 S209 Y218 D282 A312 G314 N337
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1o07, PDBe:1o07, PDBj:1o07
PDBsum1o07
PubMed12904027
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

[Back to BioLiP]