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5YCX

X-Ray Structure of Enoyl-Acyl Carrier Protein Reductase from Bacillus Anthracis with c-terminal His tag (Apo form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0030497biological_processfatty acid elongation
A0036094molecular_functionsmall molecule binding
A0042802molecular_functionidentical protein binding
A0070401molecular_functionNADP+ binding
A0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
A1902494cellular_componentcatalytic complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ATYR147

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR157

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20800575
ChainResidueDetails
ASER19
AASP66
AILE94
ALYS164
AILE193
AGLY13

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AALA97

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Involved in acyl-ACP binding => ECO:0000250
ChainResidueDetails
AASN205

220472

PDB entries from 2024-05-29

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