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5XYQ

Structure of 6-aminohexanoate-oligomer hydrolase from Arthrobacter sp. KI72., D122K 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 Residues8
Detailsbinding site for residue PO4 A 401
ChainResidue
AASP86
AALA87
AARG88
AARG88
ALYS288
ALYS288
AHOH505
AHOH680

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL B 401
ChainResidue
BARG296
BGLN299
BGLU344
BTRP347
BHOH504
BHOH568
BHOH633
BHOH683
BARG227

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL B 402
ChainResidue
ATYR98
AHOH620
BGLY90
BALA91
BVAL92
BHOH521
BHOH525
BHOH673

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL B 403
ChainResidue
ASER95
ALEU114
BSER95
BLEU114
BALA118
BHOH594

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL B 404
ChainResidue
BARG205
BARG227
BGLN251
BGLU344
BHOH514
BHOH669

site_idAC6
Number of Residues7
Detailsbinding site for residue PO4 B 405
ChainResidue
BASP86
BALA87
BARG88
BARG88
BLYS288
BHOH559
BHOH642

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

249697

PDB entries from 2026-02-25

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