Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4IIN

Crystal structure of a putative 3-oxoacyl-[acyl-carrier protein]reductase from Helicobacter pylori 26695 complexed with NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
B0006633biological_processfatty acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0051287molecular_functionNAD binding
C0000166molecular_functionnucleotide binding
C0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
C0006633biological_processfatty acid biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0051287molecular_functionNAD binding
D0000166molecular_functionnucleotide binding
D0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
D0006633biological_processfatty acid biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAD A 301
ChainResidue
AGLY12
AASN90
AALA91
AGLY92
AASN113
AVAL140
AALA141
ASER142
ATYR155
ALYS159
APRO185
ALYS15
AGLY186
AILE188
ATHR190
AHOH403
AHOH442
CGLU52
AGLY16
AILE17
AGLY18
AASN35
AARG37
AASP63
AALA64

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 302
ChainResidue
AGLU237
ATHR238
DGLU237
DTHR238
DHOH410

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD B 301
ChainResidue
BLYS15
BGLY16
BILE17
BASN35
BARG37
BASP63
BALA64
BASN90
BALA91
BGLY92
BASN113
BVAL140
BALA141
BTYR155
BLYS159
BPRO185
BGLY186
BILE188
BACT303
BHOH406
BHOH415
BHOH418
BHOH431
BHOH435

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 302
ChainResidue
BGLU237
BTHR238
CGLU237
CTHR238
CHOH420

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 303
ChainResidue
BSER142
BTYR155
BGLY186
BPHE187
BNAD301

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD C 301
ChainResidue
CGLY12
CGLY16
CILE17
CASN35
CARG37
CASP63
CALA64
CASN90
CGLY92
CVAL93
CASN113
CALA141
CSER142
CTYR155
CLYS159
CPRO185
CGLY186
CILE188
CACT302
CHOH411

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT C 302
ChainResidue
CSER142
CTYR155
CPHE187
CNAD301

site_idAC8
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAD D 301
ChainResidue
DASN113
DVAL140
DALA141
DTYR155
DLYS159
DPRO185
DGLY186
DILE188
DTHR190
DACT302
DHOH415
DGLY12
DLYS15
DGLY16
DILE17
DASN35
DARG37
DASP63
DALA64
DASN90
DGLY92
DVAL93

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT D 302
ChainResidue
DSER142
DTYR155
DGLY186
DNAD301

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SiigergnmgQtnYSASKGGMiAMSkSFA
ChainResidueDetails
ASER142-ALA170

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon