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5Y0L

Structure of 6-aminohexanoate-oligomer hydrolase from Arthrobacter sp. KI72., D122G/H130Y mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0016787molecular_functionhydrolase activity
A0019876biological_processnylon catabolic process
B0004177molecular_functionaminopeptidase activity
B0016787molecular_functionhydrolase activity
B0019876biological_processnylon catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue GOL A 1001
ChainResidue
AGLN299
AHOH1105
AHOH1203
AHOH1314

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL A 1002
ChainResidue
AARG205
AARG227
AGLU344

site_idAC3
Number of Residues5
Detailsbinding site for residue NA A 1003
ChainResidue
AHOH1328
AHOH1355
AHOH1356
AASN35
APHE38

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 B 401
ChainResidue
BARG82
BARG277
BMET278
BSER279
BPRO280

site_idAC5
Number of Residues5
Detailsbinding site for residue NA B 402
ChainResidue
BTHR315
BHOH569
BHOH583
BHOH688
BHOH741

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:29950566
ChainResidueDetails
ATHR267
BTHR267

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PDB entries from 2024-06-12

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