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5Y0M

Structure of 6-aminohexanoate-oligomer hydrolase from Arthrobacter sp. KI72., D36A/D122G/H130Y/E263Q 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 Residues9
Detailsbinding site for residue GOL A 1001
ChainResidue
AARG227
AARG296
AGLN299
AGLU344
ATRP347
AGOL1002
AHOH1152
AHOH1192
AHOH1237

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 1002
ChainResidue
AARG205
AARG227
AGLN251
AGLU344
AGOL1001
AHOH1266

site_idAC3
Number of Residues10
Detailsbinding site for residue GOL A 1003
ChainResidue
AALA91
AGLY93
AALA110
AGLY111
AVAL144
ATHR267
AHOH1139
AHOH1240
AHOH1306
BPHE134

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 1004
ChainResidue
AGLY90
AALA91
AGOL1005
AHOH1104
AHOH1264
BASP99
BLEU139

site_idAC5
Number of Residues7
Detailsbinding site for residue GOL A 1005
ChainResidue
AGLY90
AALA91
AVAL92
AGOL1004
AHOH1108
BTYR98
BASP99

site_idAC6
Number of Residues9
Detailsbinding site for residue GOL A 1006
ChainResidue
ATYR146
ALYS189
ATRP192
AASN219
AVAL221
ATHR267
AMET305
ACL1008
AHOH1306

site_idAC7
Number of Residues7
Detailsbinding site for residue PO4 A 1007
ChainResidue
AASP86
AALA87
AARG88
AARG88
ALYS288
ALYS288
AHOH1232

site_idAC8
Number of Residues4
Detailsbinding site for residue CL A 1008
ChainResidue
ATYR146
ALYS189
ATRP192
AGOL1006

site_idAC9
Number of Residues3
Detailsbinding site for residue CL A 1009
ChainResidue
AARG227
ALEU351
AHOH1336

site_idAD1
Number of Residues8
Detailsbinding site for residue GOL B 401
ChainResidue
BARG227
BARG296
BGLN299
BGLU344
BTRP347
BGOL406
BHOH543
BHOH666

site_idAD2
Number of Residues9
Detailsbinding site for residue GOL B 402
ChainResidue
ATYR98
AASP99
ALEU139
BGLY90
BALA91
BVAL92
BHOH505
BHOH639
BHOH650

site_idAD3
Number of Residues8
Detailsbinding site for residue GOL B 403
ChainResidue
BTYR146
BTRP192
BVAL221
BTHR267
BMET305
BGOL404
BCL408
BHOH686

site_idAD4
Number of Residues11
Detailsbinding site for residue GOL B 404
ChainResidue
APHE134
BALA91
BGLY93
BVAL144
BILE145
BTYR146
BASN219
BTHR267
BGOL403
BHOH552
BHOH648

site_idAD5
Number of Residues11
Detailsbinding site for residue GOL B 405
ChainResidue
ALEU114
AGLU115
BSER95
BLEU114
BGLY117
BALA118
BSER142
BHOH506
BHOH516
BHOH696
ASER95

site_idAD6
Number of Residues6
Detailsbinding site for residue GOL B 406
ChainResidue
BARG205
BARG227
BGLN251
BGLU344
BGOL401
BHOH684

site_idAD7
Number of Residues7
Detailsbinding site for residue PO4 B 407
ChainResidue
BASP86
BALA87
BARG88
BARG88
BLYS288
BLYS288
BHOH656

site_idAD8
Number of Residues4
Detailsbinding site for residue CL B 408
ChainResidue
BTYR146
BLYS189
BTRP192
BGOL403

site_idAD9
Number of Residues4
Detailsbinding site for residue CL B 409
ChainResidue
BARG127
BLEU166
BHOH629
BHOH739

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 2024-07-10

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