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5LI3

Crystal structure of HDAC-like protein from P. aeruginosa in complex with a photo-switchable inhibitor.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004407molecular_functionhistone deacetylase activity
A0016787molecular_functionhydrolase activity
A0040029biological_processepigenetic regulation of gene expression
A0046872molecular_functionmetal ion binding
B0004407molecular_functionhistone deacetylase activity
B0016787molecular_functionhydrolase activity
B0040029biological_processepigenetic regulation of gene expression
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AASP181
AHIS183
AASP269
A9RB404

site_idAC2
Number of Residues5
Detailsbinding site for residue K A 402
ChainResidue
AASP179
AASP181
AHIS183
ASER202
ALEU203

site_idAC3
Number of Residues7
Detailsbinding site for residue K A 403
ChainResidue
ATYR192
AARG195
AVAL198
ASER200
APHE227
AHOH503
AHOH527

site_idAC4
Number of Residues14
Detailsbinding site for residue 9RB A 404
ChainResidue
ATHR24
AASP101
AHIS143
AHIS144
APHE153
AASP181
AHIS183
APHE209
AASP269
ATYR313
AZN401
AHOH510
BLEU340
BPHE343

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BASP181
BHIS183
BASP269
B9RB404

site_idAC6
Number of Residues5
Detailsbinding site for residue K B 402
ChainResidue
BASP179
BASP181
BHIS183
BSER202
BLEU203

site_idAC7
Number of Residues6
Detailsbinding site for residue K B 403
ChainResidue
BTYR192
BARG195
BVAL198
BPHE227
BHOH538
BHOH553

site_idAC8
Number of Residues14
Detailsbinding site for residue 9RB B 404
ChainResidue
ALEU340
APHE343
BTHR24
BASP101
BHIS143
BHIS144
BPHE153
BASP181
BHIS183
BPHE209
BASP269
BTYR313
BZN401
BHOH502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q48935
ChainResidueDetails
AHIS144
BHIS144

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27756124, ECO:0000269|PubMed:27951649, ECO:0000312|PDB:5LI3, ECO:0007744|PDB:5G0X
ChainResidueDetails
AASP181
AHIS183
AASP269
BASP181
BHIS183
BASP269

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Polarizes the scissile carbonyl of the substrate => ECO:0000250|UniProtKB:Q48935
ChainResidueDetails
ATYR313
BTYR313

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PDB entries from 2024-11-06

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