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6LJK

Crystal structure of human Sirt5 in complex with an internally quenched fluorescent substrate GluIQF

Functional Information from GO Data
ChainGOidnamespacecontents
A0036054molecular_functionprotein-malonyllysine demalonylase activity
A0036055molecular_functionprotein-succinyllysine desuccinylase activity
A0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
ACYS166
ACYS169
ACYS207
ACYS212

site_idAC2
Number of Residues5
Detailsbinding site for residue NA A 402
ChainResidue
AALA59
AGLN140
ATHR250
ASER251
AHOH694

site_idAC3
Number of Residues8
Detailsbinding site for residue GUA B 101
ChainResidue
AARG71
ATYR102
AARG105
AHIS158
AVAL221
AHOH576
BLYS5
BHOH204

site_idAC4
Number of Residues16
Detailsbinding site for Ligand residues NIY D 7 through SET D 9 bound to SER D 6
ChainResidue
ASER65
AARG71
AGLN83
AGLU113
APRO114
AASN115
AARG119
APHE223
AVAL253
AHOH631
AHOH669
AHOH706
BSER6
BHOH201
BHOH203
BHOH207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:22076378, ECO:0000269|PubMed:29180469
ChainResidueDetails
AHIS158

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03160, ECO:0000269|PubMed:22076378, ECO:0000269|PubMed:22767592, ECO:0000269|Ref.19
ChainResidueDetails
AGLY58
AGLN140
AGLY249
AASN275
ACYS293

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03160
ChainResidueDetails
ATYR102
AARG105
ACYS166
ACYS169
ACYS207
ACYS212

219140

PDB entries from 2024-05-01

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