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5XYP

Structure of 6-aminohexanoate-oligomer hydrolase from Arthrobacter sp. KI72., D122R 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 Residues5
Detailsbinding site for residue PO4 A 401
ChainResidue
ALYS159
AHOH575
AHOH633
AHOH702
BPO4403

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL B 401
ChainResidue
BHOH592
BARG205
BARG227
BGLN251
BGLU344

site_idAC3
Number of Residues6
Detailsbinding site for residue PO4 B 402
ChainResidue
BASP86
BALA87
BARG88
BARG88
BLYS288
BHOH616

site_idAC4
Number of Residues6
Detailsbinding site for residue PO4 B 403
ChainResidue
APO4401
BLYS159
BHOH520
BHOH525
BHOH544
BHOH582

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 2024-11-06

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