Structure of PDB 2hdr Chain A

Receptor sequence

>2hdrA (length=352) Species: 83333 (Escherichia coli K-12)

APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIIIALAARPVKAITPPTPAVR
ASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNA
LQ

3D structure

• PDB: 2hdr Deconstructing fragment-based inhibitor discovery
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S64 K67 Y112 A114 V121 Y150 G156 E272 K315 A318
• Catalytic site (residue number reindexed from 1): S61 K64 Y109 A111 V118 Y147 G153 E269 K306 A309
• 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	4A3	A	V191 Y199 H210	V188 Y196 H207	MOAD: Ki=19mM PDBbind-CN: -logKd/Ki=1.72,Ki=19mM BindingDB: Ki=19000000nM
BS02	4A3	A	Q120 S212 Y221 G320	Q117 S209 Y218 G311	MOAD: Ki=19mM PDBbind-CN: -logKd/Ki=1.72,Ki=19mM BindingDB: Ki=19000000nM
BS03	4A3	A	K239 P240 L241 R309	K236 P237 L238 R300	MOAD: Ki=19mM PDBbind-CN: -logKd/Ki=1.72,Ki=19mM BindingDB: Ki=19000000nM
BS04	4A3	A	A141 W142 A143	A138 W139 A140	MOAD: Ki=19mM PDBbind-CN: -logKd/Ki=1.72,Ki=19mM BindingDB: Ki=19000000nM
BS05	4A3	A	V278 P280 W354	V275 P277 W345	MOAD: Ki=19mM PDBbind-CN: -logKd/Ki=1.72,Ki=19mM BindingDB: Ki=19000000nM
BS06	4A3	A	I48 G206	I45 G203	MOAD: Ki=19mM PDBbind-CN: -logKd/Ki=1.72,Ki=19mM BindingDB: Ki=19000000nM
BS07	4A3	A	V278 N279	V275 N276	MOAD: Ki=19mM PDBbind-CN: -logKd/Ki=1.72,Ki=19mM BindingDB: Ki=19000000nM
BS08	4A3	A	V125 K126 P213 G214 A215	V122 K123 P210 G211 A212	MOAD: Ki=19mM PDBbind-CN: -logKd/Ki=1.72,Ki=19mM BindingDB: Ki=19000000nM

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

External links

• PDB: RCSB:2hdr, PDBe:2hdr, PDBj:2hdr
• PDBsum: 2hdr
• PubMed: 17072304
• UniProt: P00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)