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1UZM

MabA from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0018454molecular_functionacetoacetyl-CoA reductase activity
A0046459biological_processshort-chain fatty acid metabolic process
A0070402molecular_functionNADPH binding
A0071768biological_processmycolic acid biosynthetic process
B0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005886cellular_componentplasma membrane
B0006633biological_processfatty acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0018454molecular_functionacetoacetyl-CoA reductase activity
B0046459biological_processshort-chain fatty acid metabolic process
B0070402molecular_functionNADPH binding
B0071768biological_processmycolic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CS A 1246
ChainResidue
APHE13
AALA37
AASP38

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CS A 1247
ChainResidue
AALA36
AALA36
AHIS40
AHIS40
AHOH2052
AHOH2052

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS B 1246
ChainResidue
BALA36
BALA36
BHIS40
BHOH2032

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS B 1247
ChainResidue
BPHE13
BALA37
BASP38
BHOH2031

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvsglwgignQanYAASKAGViGMArSIA
ChainResidueDetails
ASER140-ALA168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR153
BTYR153

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15977159, ECO:0007744|PDB:1UZN
ChainResidueDetails
AARG25
AARG47
AASP61
AGLY90
BARG25
BARG47
BASP61
BGLY90

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P71534
ChainResidueDetails
ATYR153
ALYS157
AILE186
AARG197
BTYR153
BLYS157
BILE186
BARG197

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for activity => ECO:0000305|PubMed:23006410
ChainResidueDetails
ASER140
BSER140

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609
ChainResidueDetails
ATHR2
BTHR2

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20178986
ChainResidueDetails
ATHR21
ATHR114
ATHR191
BTHR21
BTHR114
BTHR191

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ASER140
ALYS157
ATYR153

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BSER140
BLYS157
BTYR153

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ASER140
AASN112
ALYS157
ATYR153

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BSER140
BASN112
BLYS157
BTYR153

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
AGLN150
ALYS157

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BGLN150
BLYS157

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS157
ATYR153

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS157
BTYR153

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PDB entries from 2024-10-30

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