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4ZUM

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

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 Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AASP195
AHIS197
AASP284
AFKS404

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

site_idAC3
Number of Residues5
Detailsbinding site for residue NA A 403
ChainResidue
APHE206
AARG209
AVAL212
ATHR243
AHOH708

site_idAC4
Number of Residues17
Detailsbinding site for residue FKS A 404
ChainResidue
APRO156
AHIS158
AHIS159
AGLY167
ATYR168
ACYS169
AASP195
AHIS197
AASP284
AGLU320
AGLY321
ATYR323
AZN401
AHOH521
AHOH547
BTYR83
BGLU106

site_idAC5
Number of Residues7
Detailsbinding site for residue NO3 A 405
ChainResidue
AMET1
APHE45
AALA340
ANO3406
AHOH515
AHOH577
AHOH633

site_idAC6
Number of Residues6
Detailsbinding site for residue NO3 A 406
ChainResidue
AMET1
ALYS147
AALA148
ANO3405
AHOH516
AHOH717

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL A 407
ChainResidue
ALYS15
ATRP75
ALYS84
AGLY85
AHOH510

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BASP195
BHIS197
BASP284
BFKS404

site_idAC9
Number of Residues5
Detailsbinding site for residue K B 402
ChainResidue
BASP193
BASP195
BHIS197
BSER216
BLEU217

site_idAD1
Number of Residues5
Detailsbinding site for residue NA B 403
ChainResidue
BPHE206
BARG209
BVAL212
BTHR243
BHOH725

site_idAD2
Number of Residues18
Detailsbinding site for residue FKS B 404
ChainResidue
ATYR83
AGLU106
BPRO156
BHIS158
BHIS159
BGLY167
BTYR168
BCYS169
BASP195
BHIS197
BASP284
BGLU320
BGLY321
BTYR323
BZN401
BHOH526
BHOH575
BHOH778

site_idAD3
Number of Residues7
Detailsbinding site for residue NO3 B 405
ChainResidue
BMET1
BPHE45
BALA340
BNO3406
BHOH533
BHOH567
BHOH583

site_idAD4
Number of Residues6
Detailsbinding site for residue NO3 B 406
ChainResidue
BMET1
BLYS147
BALA148
BNO3405
BHOH515
BHOH731

site_idAD5
Number of Residues4
Detailsbinding site for residue GOL B 407
ChainResidue
AGLU234
AHOH594
BARG96
BHOH805

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 2024-07-17

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