Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3MEN

Crystal structure of acetylpolyamine aminohydrolase from Burkholderia pseudomallei, iodide soak

Functional Information from GO Data
ChainGOidnamespacecontents
A0004407molecular_functionhistone deacetylase activity
A0006338biological_processchromatin remodeling
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0047609molecular_functionacetylputrescine deacetylase activity
B0004407molecular_functionhistone deacetylase activity
B0006338biological_processchromatin remodeling
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0047609molecular_functionacetylputrescine deacetylase activity
C0004407molecular_functionhistone deacetylase activity
C0006338biological_processchromatin remodeling
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
C0047609molecular_functionacetylputrescine deacetylase activity
D0004407molecular_functionhistone deacetylase activity
D0006338biological_processchromatin remodeling
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
D0047609molecular_functionacetylputrescine deacetylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
AASP192
AHIS194
AASP281
ASO4401

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AASP281
ATYR320
AZN400
AHIS156
AHIS157
AGLY165
AASP192
AHIS194

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 402
ChainResidue
AASP190
AASP192
AHIS194
ASER213
AILE214

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 343
ChainResidue
AHIS13
AGLU120

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD A 345
ChainResidue
ASER19
AARG20
BASN91

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 346
ChainResidue
AASN91

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 347
ChainResidue
ASER19
ASER115

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 348
ChainResidue
AGLN106
AHOH453

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 349
ChainResidue
AHOH480

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 400
ChainResidue
CASP192
CHIS194
CASP281
CSO4401

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 C 401
ChainResidue
CHIS156
CHIS157
CGLY165
CASP192
CHIS194
CASP281
CGLY318
CTYR320
CZN400

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K C 402
ChainResidue
CASP190
CASP192
CHIS194
CSER213
CILE214

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD C 342
ChainResidue
CPRO247

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD C 343
ChainResidue
CHIS13
CGLU120
CHIS121

site_idBC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD C 344
ChainResidue
CTHR72

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD C 345
ChainResidue
CSER19
DASN91

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD C 348
ChainResidue
CSER19
CSER115

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 400
ChainResidue
BASP192
BHIS194
BASP281
BSO4401

site_idCC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 401
ChainResidue
BHIS156
BHIS157
BGLY165
BASP192
BHIS194
BASP281
BTYR320
BZN400

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 402
ChainResidue
BASP190
BASP192
BHIS194
BSER213
BILE214

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 403
ChainResidue
BARG22
BARG24
BMET25
BHOH483
DARG48

site_idCC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD B 344
ChainResidue
BHIS13
BGLU120

site_idCC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 347
ChainResidue
BSER115

site_idCC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD B 348
ChainResidue
BGLN200
BHOH424

site_idCC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 350
ChainResidue
BHOH420

site_idCC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 400
ChainResidue
DASP192
DHIS194
DASP281
DSO4401

site_idCC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 D 401
ChainResidue
DHIS156
DHIS157
DGLY165
DASP192
DHIS194
DASP281
DTYR320
DZN400

site_idDC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K D 402
ChainResidue
DILE214
DASP190
DASP192
DHIS194
DSER213

site_idDC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 D 403
ChainResidue
DARG24
DMET25

site_idDC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD D 343
ChainResidue
DSER19

site_idDC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD D 346
ChainResidue
DHIS13

site_idDC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD D 347
ChainResidue
DHOH360

site_idDC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD D 349
ChainResidue
DSER19
DSER115

site_idDC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IOD D 350
ChainResidue
DARG141
DLEU179
DARG182
DHIS183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q48935
ChainResidueDetails
AHIS157
BHIS157
CHIS157
DHIS157

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:21359836, ECO:0007744|PDB:3MEN
ChainResidueDetails
AASP192
DASP192
DHIS194
DASP281
AHIS194
AASP281
BASP192
BHIS194
BASP281
CASP192
CHIS194
CASP281

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Polarizes the scissile carbonyl of the substrate => ECO:0000250|UniProtKB:Q48935
ChainResidueDetails
ATYR320
BTYR320
CTYR320
DTYR320

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon