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5XYS

Structure of 6-aminohexanoate-oligomer hydrolase from Arthrobacter sp. KI72., D122V 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 Residues6
Detailsbinding site for residue GOL A 401
ChainResidue
AARG205
AARG227
AGLN251
AGLU344
AHOH515
AHOH651

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 402
ChainResidue
AHOH508
AHOH509
AHOH594
AHOH629
AARG227
AGLN299
ATRP347

site_idAC3
Number of Residues6
Detailsbinding site for residue PO4 A 403
ChainResidue
AASP86
AALA87
AARG88
AARG88
ALYS288
AHOH639

site_idAC4
Number of Residues7
Detailsbinding site for residue PO4 B 401
ChainResidue
BASP86
BALA87
BARG88
BARG88
BLYS288
BLYS288
BHOH630

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"29950566","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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