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5VM2

Crystal structure of ECK1772, an oxidoreductase/dehydrogenase of unknown specificity involved in membrane biogenesis from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MG A 401
ChainResidue
AHIS65
AGLU66
AGLU152
AHOH705

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 402
ChainResidue
ACYS95
ACYS98
ACYS101
ACYS109

site_idAC3
Number of Residues5
Detailsbinding site for residue MG B 401
ChainResidue
BHIS65
BGLU66
BGLU152
BHOH650
BCSO39

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 402
ChainResidue
BCYS95
BCYS98
BCYS101
BCYS109

site_idAC5
Number of Residues6
Detailsbinding site for residue CL B 403
ChainResidue
BLYS312
BLYS312
BSER313
BSER313
BVAL315
BVAL315

Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEcAGTvvavGsrV
ChainResidueDetails
AGLY64-VAL78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ACSO39
BCYS95
BCYS98
BCYS101
BCYS109
BGLU152
AHIS65
ACYS95
ACYS98
ACYS101
ACYS109
AGLU152
BCSO39
BHIS65

225946

PDB entries from 2024-10-09

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