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2GV1

NMR solution structure of the Acylphosphatase from Eschaerichia Coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0003998molecular_functionacylphosphatase activity
A0009408biological_processresponse to heat
A0016787molecular_functionhydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00150
Number of Residues11
DetailsACYLPHOSPHATASE_1 Acylphosphatase signature 1. VyGrVQGVgFR
ChainResidueDetails
AVAL10-ARG20

site_idPS00151
Number of Residues17
DetailsACYLPHOSPHATASE_2 Acylphosphatase signature 2. GYAKNlddGsVevvacG
ChainResidueDetails
AGLY34-GLY50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01450
ChainResidueDetails
AARG20
AASN38

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2acy
ChainResidueDetails
AASN38
AARG20

222624

PDB entries from 2024-07-17

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