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4LXZ

Structure of Human HDAC2 in complex with SAHA (vorinostat)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004407molecular_functionhistone deacetylase activity
B0004407molecular_functionhistone deacetylase activity
C0004407molecular_functionhistone deacetylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AASP181
AHIS183
AASP269
ASHH407

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AASP179
AASP181
AHIS183
ASER202
APHE203

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 403
ChainResidue
APHE192
ATHR195
AVAL198
ATYR227
AHOH522
AHOH528

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PG4 A 404
ChainResidue
ALYS71
AALA191

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 A 405
ChainResidue
AARG311
AGLU340
ATYR341
AGLY343

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 A 406
ChainResidue
AASP23
AASN26
ATYR27
AASP109
AHOH802

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SHH A 407
ChainResidue
APRO34
AASP104
AHIS145
AHIS146
AGLY154
APHE155
AASP181
AHIS183
AASP269
ATYR308
AZN401
AHOH606
AHOH791

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BASP181
BHIS183
BASP269
BSHH408

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BASP179
BASP181
BHIS183
BSER202
BPHE203

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 403
ChainResidue
BPHE192
BTHR195
BVAL198
BTYR227
BHOH533
BHOH549

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NHE B 404
ChainResidue
ATYR59
ALYS128
BASP21
BASP23
BARG60
BLYS63
BGLU113

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 B 405
ChainResidue
BARG311
BGLU340
BTYR341
BGLY343
BHOH835

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 B 406
ChainResidue
BLYS284
BASN331
BHIS349
CGLU67
CTHR70

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PG4 B 407
ChainResidue
AARG131
BASP23
BASN26
BTYR27
BASP109
BGLU113

site_idBC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SHH B 408
ChainResidue
BPRO34
BASP104
BHIS145
BHIS146
BGLY154
BASP181
BHIS183
BASP269
BTYR308
BZN401
BHOH671

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 401
ChainResidue
CASP181
CHIS183
CASP269
CSHH406

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 402
ChainResidue
CASP179
CASP181
CHIS183
CSER202
CPHE203

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA C 403
ChainResidue
CVAL198
CTYR227
CHOH505
CHOH520
CPHE192
CTHR195

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PG4 C 404
ChainResidue
BPRO344
BASP345
CALA191
CARG197
CHOH540
CHOH627

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 C 405
ChainResidue
BASN354
CLEU169
CTYR171
CGLN173
CARG197

site_idCC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SHH C 406
ChainResidue
CPRO34
CASP104
CHIS145
CHIS146
CGLY154
CASP181
CHIS183
CASP269
CTYR308
CHIS380
CZN401
CHOH641
CHOH755

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q13547
ChainResidueDetails
AHIS146
BHIS146
CHIS146

site_idSWS_FT_FI2
Number of Residues27
DetailsBINDING: BINDING => ECO:0000269|PubMed:37137925, ECO:0007744|PDB:8BPA, ECO:0007744|PDB:8BPB, ECO:0007744|PDB:8BPC
ChainResidueDetails
AASP179
BASP179
BASP181
BHIS183
BPHE192
BTHR195
BVAL198
BSER202
BPHE203
BASP269
CASP179
AASP181
CASP181
CHIS183
CPHE192
CTHR195
CVAL198
CSER202
CPHE203
CASP269
AHIS183
APHE192
ATHR195
AVAL198
ASER202
APHE203
AASP269

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:37137925, ECO:0007744|PDB:8BPB, ECO:0007744|PDB:8BPC
ChainResidueDetails
ATYR227
BTYR227
CTYR227

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q13547
ChainResidueDetails
ALYS79
BLYS79
CLYS79

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q13547
ChainResidueDetails
ALYS225
BLYS225
CLYS225

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P70288
ChainResidueDetails
ACYS266
ACYS278
BCYS266
BCYS278
CCYS266
CCYS278

site_idSWS_FT_FI7
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS79
BLYS79
CLYS79

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PDB entries from 2024-05-01

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