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5OVJ

Structure of the apo form of Mycobacterium smegmatis MabA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
A0005576cellular_componentextracellular region
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0018454molecular_functionacetoacetyl-CoA reductase activity
A0030497biological_processfatty acid elongation
A0050661molecular_functionNADP binding
B0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
B0005576cellular_componentextracellular region
B0006633biological_processfatty acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0018454molecular_functionacetoacetyl-CoA reductase activity
B0030497biological_processfatty acid elongation
B0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 A 301
ChainResidue
ATHR109
AARG112
AHOH409
AHOH491

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 302
ChainResidue
AHOH545
BHOH408
AASN32
AARG33
AARG55
AGLY56
ASER57

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 303
ChainResidue
ATHR109
AGLU110
AGLU111
AHOH405
AHOH416

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 304
ChainResidue
AARG18
APRO19
AHOH440
BARG18
BHOH492

site_idAC5
Number of Residues7
Detailsbinding site for residue SO4 B 301
ChainResidue
BASN32
BARG33
BHIS54
BARG55
BGLY56
BSER57
BHOH416

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 B 302
ChainResidue
AARG200
BARG78
BHOH463

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 B 303
ChainResidue
BTHR109
BARG112
BHOH402

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvsgmwgignQanYAAAKAGLiGMArSIS
ChainResidueDetails
ASER148-SER176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR161
BTYR161

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:29717709
ChainResidueDetails
AASP69
ATYR161
ALYS165
AILE194
AARG205
BASN32
BARG55
BASP69
BTYR161
BLYS165
BILE194
BARG205
AASN32
AARG55

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WGT3
ChainResidueDetails
AGLY98
BGLY98

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for activity => ECO:0000250|UniProtKB:P9WGT3
ChainResidueDetails
ASER148
BSER148

219869

PDB entries from 2024-05-15

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