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1ZZ0

Crystal structure of a HDAC-like protein with acetate bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1451
ChainResidue
AASP180
AHIS182
AASP268
AACT1452

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1551
ChainResidue
BASP180
BHIS182
BASP268
BACT1552

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1651
ChainResidue
CHIS182
CASP268
CACT1652
CASP180

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1751
ChainResidue
DASP180
DHIS182
DASP268
DACT1752

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 1449
ChainResidue
AASP178
AASP180
AHIS182
ASER201
ALEU202

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K A 1450
ChainResidue
ATRP191
AASP194
AVAL197
ATHR199
ATYR226
AHOH1463
AHOH1476

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 1549
ChainResidue
BASP178
BASP180
BHIS182
BSER201
BLEU202

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 1550
ChainResidue
BTRP191
BASP194
BVAL197
BTYR226
BHOH1555
BHOH1584

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K C 1649
ChainResidue
CASP178
CASP180
CHIS182
CSER201
CLEU202

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K C 1650
ChainResidue
CTRP191
CASP194
CVAL197
CTYR226
CHOH1658
CHOH1671

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K D 1749
ChainResidue
DTRP191
DASP194
DVAL197
DTHR199
DTYR226
DHOH1784
DHOH1785

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K D 1750
ChainResidue
DASP178
DASP180
DHIS182
DSER201
DLEU202

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT A 1452
ChainResidue
AHIS142
AHIS143
AGLY151
AASP180
AHIS182
AASP268
AGLY310
ATYR312
AZN1451

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT B 1552
ChainResidue
BHIS142
BHIS143
BGLY151
BASP180
BHIS182
BASP268
BGLY310
BTYR312
BZN1551

site_idBC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT C 1652
ChainResidue
CHIS142
CHIS143
CGLY151
CASP180
CHIS182
CASP268
CGLY310
CTYR312
CZN1651

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT D 1752
ChainResidue
DHIS142
DHIS143
DGLY151
DASP180
DHIS182
DASP268
DGLY310
DTYR312
DZN1751

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q48935
ChainResidueDetails
AALA144
BALA144
CALA144
DALA144

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:27756124, ECO:0007744|PDB:5G1C
ChainResidueDetails
AVAL181
DVAL181
DHIS183
DALA269
AHIS183
AALA269
BVAL181
BHIS183
BALA269
CVAL181
CHIS183
CALA269

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Polarizes the scissile carbonyl of the substrate => ECO:0000250|UniProtKB:Q48935
ChainResidueDetails
ASER313
BSER313
CSER313
DSER313

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PDB entries from 2024-07-24

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