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4FS3

Crystal structure of Staphylococcus aureus enoyl-ACP reductase in complex with NADP and AFN-1252

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
A0042802molecular_functionidentical protein binding
A0050661molecular_functionNADP binding
A0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE 0WD A 301
ChainResidue
AGLY13
AASP66
AVAL67
ASER93
AILE94
AALA95
AILE120
ATHR145
ATHR146
ATYR147
ALYS164
AILE14
AALA190
AGLY191
APRO192
AILE193
ATHR195
ALEU196
ASER197
A0WE302
AHOH408
AHOH424
AALA15
AHOH472
AHOH473
AHOH567
AHOH598
AHOH634
ASER19
AILE20
ATHR38
ATYR39
AARG40
AILE65

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 0WE A 302
ChainResidue
APHE96
AALA97
ALEU102
ATYR147
AGLN155
AASN156
ATYR157
ASER197
A0WD301
AHOH526

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ATYR147
ATYR157

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:19768684
ChainResidueDetails
AGLY13
ASER19
AARG40
AASP66
AILE94
ALYS164
AILE193

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AALA97

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Critical for cofactor specificity => ECO:0000250
ChainResidueDetails
AARG40
ALYS41

222415

PDB entries from 2024-07-10

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