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1GQZ

Refinement of Haemophilus influenzae Diaminopimelate epimerase at 1.7A

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0008837molecular_functiondiaminopimelate epimerase activity
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016853molecular_functionisomerase activity
Functional Information from PROSITE/UniProt
site_idPS01326
Number of Residues15
DetailsDAP_EPIMERASE Diaminopimelate epimerase signature. NaDGSevsqCGNGaR
ChainResidueDetails
AASN64-ARG78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:16723397, ECO:0000305|PubMed:9843410, ECO:0000305|DOI:10.1021/ja001193t, ECO:0007744|PDB:1BWZ, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ
ChainResidueDetails
ACYS73

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:16723397, ECO:0000305|PubMed:9843410, ECO:0000305|DOI:10.1021/ja001193t, ECO:0007744|PDB:1BWZ, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ
ChainResidueDetails
ACYS217

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ
ChainResidueDetails
AASN11
AASN64
AGLY74
AASN157
AASN190
AGLU208
AGLY218

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKJ
ChainResidueDetails
AGLN44

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000305|PubMed:9843410, ECO:0007744|PDB:1BWZ
ChainResidueDetails
AHIS159
AGLU208

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for dimerization => ECO:0000250|UniProtKB:P0A6K1
ChainResidueDetails
ATYR268

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 334
ChainResidueDetails
ACYS73hydrogen bond acceptor, proton acceptor
AHIS159activator, electrostatic stabiliser
AGLU208activator, electrostatic stabiliser
ACYS217hydrogen bond donor, proton donor
AGLY220electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-04-10

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