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5JAQ

Yersinia pestis FabV variant T276C

Functional Information from GO Data
ChainGOidnamespacecontents
A0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0050343molecular_functiontrans-2-enoyl-CoA reductase (NADH) activity
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues32
Detailsbinding site for residue NAI A 401
ChainResidue
AGLY48
AGLY110
AASP111
AALA112
ASER138
ALEU139
AALA140
ASER141
APHE223
ATHR224
ATYR225
AALA49
ALEU271
ALYS272
AALA273
AVAL274
ACYS276
ADMS403
AHOH535
AHOH541
AHOH562
AHOH586
ASER50
AHOH625
AHOH637
AHOH656
ATHR51
AGLY52
ATYR53
APHE73
APHE74
AGLU75

site_idAC2
Number of Residues5
Detailsbinding site for residue DMS A 402
ChainResidue
ALYS26
AASN372
AGLY377
AILE378
AASP379

site_idAC3
Number of Residues4
Detailsbinding site for residue DMS A 403
ChainResidue
ATYR225
ATYR235
ANAI401
AHOH544

site_idAC4
Number of Residues7
Detailsbinding site for residue DMS A 404
ChainResidue
AGLU79
AGLU80
ALYS106
AASP390
AASN395
AILE397
AHOH568

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01838, ECO:0000305|PubMed:22244758
ChainResidueDetails
ATYR235

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:22244758, ECO:0000269|Ref.5
ChainResidueDetails
AGLY48
APHE74
AASP111
ALYS244
AVAL274

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01838
ChainResidueDetails
ALEU139
ATYR225

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Plays an important role in discriminating NADH against NADPH => ECO:0000255|HAMAP-Rule:MF_01838
ChainResidueDetails
AGLU75

218853

PDB entries from 2024-04-24

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