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4ZUP

Crystal structure of acetylpolyamine amidohydrolase from Mycoplana ramosa in complex with a hydroxamate 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
A5XA405

site_idAC2
Number of Residues2
Detailsbinding site for residue ZN A 402
ChainResidue
AHIS146
ANO3408

site_idAC3
Number of Residues5
Detailsbinding site for residue K A 403
ChainResidue
ASER216
ALEU217
AASP193
AASP195
AHIS197

site_idAC4
Number of Residues5
Detailsbinding site for residue K A 404
ChainResidue
APHE206
AARG209
AVAL212
ATHR243
AHOH609

site_idAC5
Number of Residues12
Detailsbinding site for residue 5XA A 405
ChainResidue
AGLU117
AHIS158
AHIS159
ATYR168
AASP195
AHIS197
APHE225
AASP284
ATYR323
AZN401
AHOH729
BHOH646

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 406
ChainResidue
ALYS15
ATRP75
ALYS84
AGLY85
AHOH531
AHOH712

site_idAC7
Number of Residues7
Detailsbinding site for residue NO3 A 407
ChainResidue
AMET1
APHE45
AALA340
ANO3408
AHOH504
AHOH536
AHOH557

site_idAC8
Number of Residues9
Detailsbinding site for residue NO3 A 408
ChainResidue
AMET1
AHIS146
ALYS147
AALA148
AZN402
ANO3407
AHOH557
AHOH564
AHOH755

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL A 409
ChainResidue
ATYR231
AALA232
AGLU233
AHOH513
AHOH554
AHOH769
BARG100

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BASP195
BHIS197
BASP284
B5XA405

site_idAD2
Number of Residues2
Detailsbinding site for residue ZN B 402
ChainResidue
BHIS146
BNO3408

site_idAD3
Number of Residues5
Detailsbinding site for residue K B 403
ChainResidue
BASP193
BASP195
BHIS197
BSER216
BLEU217

site_idAD4
Number of Residues5
Detailsbinding site for residue K B 404
ChainResidue
BPHE206
BARG209
BVAL212
BTHR243
BHOH610

site_idAD5
Number of Residues13
Detailsbinding site for residue 5XA B 405
ChainResidue
BGLU117
BHIS158
BHIS159
BGLY167
BTYR168
BASP195
BHIS197
BPHE225
BASP284
BTYR323
BZN401
BHOH536
BHOH751

site_idAD6
Number of Residues6
Detailsbinding site for residue GOL B 406
ChainResidue
AHOH529
AHOH559
BARG96
BHOH502
BHOH765
BHOH789

site_idAD7
Number of Residues7
Detailsbinding site for residue NO3 B 407
ChainResidue
BMET1
BPHE45
BALA340
BNO3408
BHOH513
BHOH544
BHOH562

site_idAD8
Number of Residues9
Detailsbinding site for residue NO3 B 408
ChainResidue
BMET1
BHIS146
BLYS147
BALA148
BZN402
BNO3407
BHOH501
BHOH562
BHOH700

site_idAD9
Number of Residues10
Detailsbinding site for residue GOL B 409
ChainResidue
BLEU266
BTHR307
BALA310
BSER311
BHOH512
BHOH531
BHOH566
BHOH723
BHOH793
BHOH868

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 2024-06-19

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