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3ISZ

Crystal structure of mono-zinc form of succinyl-diaminopimelate desuccinylase from Haemophilus influenzae

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0009014molecular_functionsuccinyl-diaminopimelate desuccinylase activity
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016787molecular_functionhydrolase activity
A0019877biological_processdiaminopimelate biosynthetic process
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0009014molecular_functionsuccinyl-diaminopimelate desuccinylase activity
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0016787molecular_functionhydrolase activity
B0019877biological_processdiaminopimelate biosynthetic process
B0046872molecular_functionmetal ion binding
B0050897molecular_functioncobalt ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AHIS67
AASP100
AGLU163
AHOH572

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 378
ChainResidue
AHOH587
AHOH588
AARG178
AARG179
AGLY322
AHOH552
AHOH580

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1001
ChainResidue
BHIS67
BASP100
BGLU163
BHOH420

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 378
ChainResidue
BARG178
BARG179
BARG258
BGLY322
BHOH419
BHOH491

Functional Information from PROSITE/UniProt
site_idPS00758
Number of Residues10
DetailsARGE_DAPE_CPG2_1 ArgE / dapE / ACY1 / CPG2 / yscS family signature 1. IAFAGHtDVV
ChainResidueDetails
AILE62-VAL71

site_idPS00759
Number of Residues40
DetailsARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. AADmKGslAamIvaaeeyvkanpnhkgt.IaLLItsDEEaT
ChainResidueDetails
AALA98-THR137

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:20138056
ChainResidueDetails
AASP69
BASP69

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:20138056
ChainResidueDetails
AGLU134
BGLU134

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20138056, ECO:0007744|PDB:3IC1, ECO:0007744|PDB:3ISZ, ECO:0007744|PDB:4H2K
ChainResidueDetails
AHIS67
AGLU163
BHIS67
BGLU163

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20138056, ECO:0007744|PDB:3IC1, ECO:0007744|PDB:4H2K
ChainResidueDetails
AASP100
AGLU135
AHIS349
BASP100
BGLU135
BHIS349

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
AGLU134

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
BGLU134

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
AGLU135
AASP100
AHIS349
AGLU134
AHIS67
AGLU163

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
BGLU135
BASP100
BHIS349
BGLU134
BHIS67
BGLU163

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PDB entries from 2024-08-21

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