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5XYG

Structure of 6-aminohexanoate-oligomer hydrolase from Arthrobacter sp. KI72.

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 Residues3
Detailsbinding site for residue GOL A 401
ChainResidue
AGLN299
AHOH518
AHOH543

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 402
ChainResidue
BALA118
ASER95
ALEU114
AALA118
AHOH537
BSER95
BLEU114

site_idAC3
Number of Residues2
Detailsbinding site for residue SO4 A 403
ChainResidue
AALA160
AARG163

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 404
ChainResidue
AGLU49
AMET50
AARG52

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 405
ChainResidue
ATYR146
ALYS189
AHOH673

site_idAC6
Number of Residues2
Detailsbinding site for residue CL A 406
ChainResidue
AARG227
ALEU351

site_idAC7
Number of Residues4
Detailsbinding site for residue SO4 B 401
ChainResidue
BARG82
BMET278
BSER279
BPRO280

site_idAC8
Number of Residues3
Detailsbinding site for residue CL B 402
ChainResidue
BTYR146
BLYS189
BHOH653

site_idAC9
Number of Residues3
Detailsbinding site for residue CL B 403
ChainResidue
BARG227
BLEU351
BHOH685

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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