Structure of PDB 3a2q Chain A

Receptor sequence
>3a2qA (length=482) [Search protein sequence]
VDLWQDATAQAELVRSGEISRTELLEATIAHVQAVNPEINAVIIPLFEKA
RRESELASGPFAGVPYLLKDLTVVSQGDINTSSIKGMKESGYRADHDAYF
VQRMRAAGFVLLGKTNTPEMGNQVTTEPEAWGATRNPWNLGRSVGGSSGG
SGAAVAAALSPVAHGNDAAGAVRIPASVCGVVGLKPTRGRISPGPLVTDS
DNVAGAAHEGLFARSVRDIAALLDVVSGHRPGDTFCAPTASRPYAQGISE
NPGSLRVGVLTHNPVGDFALDPECAAAARGAAAALAALGHDVNDAYPEAL
GDRSFLKDYSTICDVAIAREIERNGELIGRPLTEDDVEWTSWEMVKRADQ
VTGRAFAACVDELRYYAGKVERWWEAGWDLLILPTVTRQTPEIGELMLAK
GTDLEGRQSAFISGSLQMLAFTVPFNVSGQPAISLPIGMSSDGMPIGVQI
VAAYGREDLLLQVAAQLEGALPWVARRPQLLN
3D structure
PDB3a2q X-ray crystallographic analysis of the 6-aminohexanoate cyclic dimer hydrolase: catalytic mechanism and evolution of an enzyme responsible for nylon-6 byproduct degradation
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K72 S150 S151 N169 A171 A172 G173 A174 I177
Catalytic site (residue number reindexed from 1) K69 S147 S148 N166 A168 A169 G170 A171 I174
Enzyme Commision number 3.5.2.12: 6-aminohexanoate-cyclic-dimer hydrolase.
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 ACA A G124 N125 S150 A171 G121 N122 S147 A168
BS02 ACA A G124 A171 A172 A174 C316 G121 A168 A169 A171 C313
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
GO:0019874 6-aminohexanoate-cyclic-dimer hydrolase activity
Biological Process
GO:0019876 nylon catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3a2q, PDBe:3a2q, PDBj:3a2q
PDBsum3a2q
PubMed19889645
UniProtP13398|NYLA_PAEUR 6-aminohexanoate-cyclic-dimer hydrolase (Gene Name=nylA)

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