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4H2K

Crystal structure of the catalytic domain of succinyl-diaminopimelate desuccinylase from Haemophilus influenzae

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AHIS67
AASP100
AGLU134
AGLU163
AZN1002
AHOH1101

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1002
ChainResidue
AZN1001
AHOH1101
AASP100
AGLU135
AHIS238

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 1001
ChainResidue
BHIS67
BASP100
BGLU134
BGLU163
BZN1002
BHOH1101

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 1002
ChainResidue
BASP100
BGLU135
BHIS238
BZN1001
BHOH1101

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
AHIS238
BASP100
BGLU135
BHIS238

223532

PDB entries from 2024-08-07

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