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1K77

Crystal Structure of EC1530, a Putative Oxygenase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0008903molecular_functionhydroxypyruvate isomerase activity
A0016853molecular_functionisomerase activity
A0046487biological_processglyoxylate metabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 300
ChainResidue
AGLU143
AASP178
AGLN204
AGLU240
AFMT304
AHOH469

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AASP186
AHOH326
AHOH326
AVAL185
AVAL185
AASP186

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
APRO2
APHE4
APHE29
AASP30
AHOH433

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
ASER9
APHE17
AARG20
ALEU35
APHE36
ATYR40
AHOH407
AHOH454
AHOH529
AHOH560

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 304
ChainResidue
AGLU143
AVAL149
AASP178
AHIS181
AARG211
AGLU240
AMG300
AHOH446

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q9WYP7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12112708","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K77","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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