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4ZUN

Crystal structure of acetylpolyamine amidohydrolase from Mycoplana ramosa in complex with a thiol 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 Residues19
Detailsbinding site for residue SS9 A 401
ChainResidue
ATYR19
ATYR323
AZN404
AZN405
AHOH513
AHOH542
AHOH546
AHOH662
AHOH793
BTYR83
BGLU106
AHIS158
AHIS159
AGLY167
ATYR168
AASP195
AHIS197
AASP284
AILE291

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
AHOH706

site_idAC4
Number of Residues5
Detailsbinding site for residue ZN A 404
ChainResidue
AASP195
AHIS197
AASP284
ASS9401
AZN405

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN A 405
ChainResidue
AHIS158
AHIS159
ASS9401
AZN404
AHOH793

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL A 406
ChainResidue
ALYS15
ATRP75
ALYS84
AGLY85
AHOH514

site_idAC7
Number of Residues5
Detailsbinding site for residue K B 401
ChainResidue
BASP193
BASP195
BHIS197
BSER216
BLEU217

site_idAC8
Number of Residues5
Detailsbinding site for residue NA B 402
ChainResidue
BPHE206
BARG209
BVAL212
BTHR243
BHOH673

site_idAC9
Number of Residues5
Detailsbinding site for residue ZN B 403
ChainResidue
BASP195
BHIS197
BASP284
BZN404
BSS9405

site_idAD1
Number of Residues5
Detailsbinding site for residue ZN B 404
ChainResidue
BHIS158
BHIS159
BZN403
BSS9405
BHOH804

site_idAD2
Number of Residues19
Detailsbinding site for residue SS9 B 405
ChainResidue
ATYR83
AGLU106
BHIS158
BHIS159
BGLY167
BTYR168
BASP195
BHIS197
BPHE225
BASP284
BGLY321
BTYR323
BZN403
BZN404
BHOH504
BHOH513
BHOH534
BHOH553
BHOH804

site_idAD3
Number of Residues5
Detailsbinding site for residue GOL B 406
ChainResidue
BLYS15
BTRP75
BLYS84
BGLY85
BHOH523

site_idAD4
Number of Residues4
Detailsbinding site for residue GOL B 407
ChainResidue
AHOH567
BARG96
BSER98
BHOH743

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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