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4ZUO

Crystal structure of acetylpolyamine amidohydrolase from Mycoplana ramosa in complex with a hydroxamate inhibitor

Replaces:  4K6Q
Functional Information from GO Data
ChainGOidnamespacecontents
A0004407molecular_functionhistone deacetylase activity
A0006338biological_processchromatin remodeling
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0047609molecular_functionacetylputrescine deacetylase activity
A0047611molecular_functionacetylspermidine deacetylase activity
B0004407molecular_functionhistone deacetylase activity
B0006338biological_processchromatin remodeling
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0047609molecular_functionacetylputrescine deacetylase activity
B0047611molecular_functionacetylspermidine deacetylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ZN A 401
ChainResidue
AASP195
AHIS197
AASP284
AXS6404
AHOH511
AHOH557

site_idAC2
Number of Residues5
Detailsbinding site for residue K A 402
ChainResidue
ASER216
ALEU217
AASP193
AASP195
AHIS197

site_idAC3
Number of Residues5
Detailsbinding site for residue NH4 A 403
ChainResidue
APHE206
AARG209
AVAL212
ATHR243
AHOH606

site_idAC4
Number of Residues17
Detailsbinding site for residue XS6 A 404
ChainResidue
ATYR19
AHIS158
AHIS159
ATYR168
AASP195
AHIS197
APHE225
AASP284
ATYR323
AZN401
AHOH511
AHOH557
AHOH645
AHOH756
AHOH800
BTYR83
BHOH843

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 405
ChainResidue
AARG96
AHOH502
BHOH550

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL A 406
ChainResidue
ALYS15
ATRP75
ALYS84
AGLY85
AHOH521

site_idAC7
Number of Residues6
Detailsbinding site for residue ZN B 401
ChainResidue
BASP195
BHIS197
BASP284
BXS6404
BHOH539
BHOH541

site_idAC8
Number of Residues5
Detailsbinding site for residue K B 402
ChainResidue
BASP193
BASP195
BHIS197
BSER216
BLEU217

site_idAC9
Number of Residues7
Detailsbinding site for residue NH4 B 403
ChainResidue
BPHE206
BARG209
BVAL212
BTHR243
BTHR244
BHOH612
BHOH684

site_idAD1
Number of Residues16
Detailsbinding site for residue XS6 B 404
ChainResidue
ATYR83
BHIS158
BHIS159
BGLY167
BTYR168
BASP195
BHIS197
BPHE225
BASP284
BTYR323
BZN401
BHOH539
BHOH541
BHOH574
BHOH785
BHOH795

site_idAD2
Number of Residues3
Detailsbinding site for residue GOL B 405
ChainResidue
AHOH553
BARG96
BHOH504

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL B 406
ChainResidue
BLYS15
BLYS84
BGLY85
BHOH532
BHOH647
BHOH687

site_idAD4
Number of Residues8
Detailsbinding site for residue GOL B 407
ChainResidue
BALA245
BASN246
BTYR247
BARG268
BHOH503
BHOH507
BHOH508
BHOH650

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:21268586, ECO:0000305|PubMed:26200446
ChainResidueDetails
AHIS159
BHIS159

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21268586, ECO:0007744|PDB:3Q9E
ChainResidueDetails
ATYR19
AGLU117
ATYR323
BTYR19
BGLU117
BTYR323

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21268586, ECO:0007744|PDB:3Q9C
ChainResidueDetails
AGLU106
BGLU106

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21268586, ECO:0000269|PubMed:26200446, ECO:0007744|PDB:3Q9B, ECO:0007744|PDB:3Q9E
ChainResidueDetails
AASP195
AHIS197
AASP284
BASP195
BHIS197
BASP284

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Polarizes the scissile carbonyl of the substrate => ECO:0000305|PubMed:21268586
ChainResidueDetails
ATYR323
BTYR323

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PDB entries from 2024-09-04

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