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5MSU

Structure of the R domain of carboxylic acid reductase (CAR) from Mycobacterium marinum in complex with NADP, P21 form

Functional Information from GO Data
ChainGOidnamespacecontents
A0001676biological_processlong-chain fatty acid metabolic process
A0004467molecular_functionlong-chain fatty acid-CoA ligase activity
A0005524molecular_functionATP binding
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0009058biological_processbiosynthetic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0031177molecular_functionphosphopantetheine binding
A0050661molecular_functionNADP binding
B0001676biological_processlong-chain fatty acid metabolic process
B0004467molecular_functionlong-chain fatty acid-CoA ligase activity
B0005524molecular_functionATP binding
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0009058biological_processbiosynthetic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0031177molecular_functionphosphopantetheine binding
B0050661molecular_functionNADP binding
C0001676biological_processlong-chain fatty acid metabolic process
C0004467molecular_functionlong-chain fatty acid-CoA ligase activity
C0005524molecular_functionATP binding
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0009058biological_processbiosynthetic process
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0031177molecular_functionphosphopantetheine binding
C0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues36
Detailsbinding site for residue NAP C 1201
ChainResidue
ALYS816
CLYS855
CPRO880
CALA881
CALA882
CVAL884
CTHR919
CSER920
CTYR956
CLYS960
CCYS983
CGLY785
CASP984
CILE986
CASN997
CHOH1331
CHOH1353
CHOH1363
CHOH1369
CHOH1378
CHOH1380
CHOH1421
CTHR787
CHOH1427
CHOH1453
CHOH1485
CHOH1510
CHOH1513
CHOH1520
CHOH1552
CGLY788
CPHE789
CLEU790
CARG814
CARG824
CASP854

site_idAC2
Number of Residues34
Detailsbinding site for residue NAP A 1601
ChainResidue
AGLY785
ATHR787
AGLY788
APHE789
ALEU790
AARG814
AARG824
AASP854
ALYS855
APRO880
AALA881
AALA882
AVAL884
ATHR919
ASER920
ATYR956
ALYS960
ACYS983
AASP984
AMET985
AILE986
AASN997
AHOH1720
AHOH1740
AHOH1760
AHOH1774
AHOH1776
AHOH1785
AHOH1786
AHOH1789
AHOH1825
AHOH1857
AHOH1869
AHOH1898

site_idAC3
Number of Residues23
Detailsbinding site for residue NAP B 1201
ChainResidue
BGLY785
BTHR787
BGLY788
BPHE789
BLEU790
BGLY791
BARG814
BARG824
BASP854
BLYS855
BPRO880
BALA881
BALA882
BTHR919
BTYR956
BLYS960
BHOH1394
BHOH1462
BHOH1466
BHOH1491
BHOH1499
BHOH1506
BHOH1554

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SatravddsyAngYSNSKWAGeVLLrEAH
ChainResidueDetails
CSER943-HIS971

site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. LIYTSGSTGaPK
ChainResidueDetails
CLEU250-LYS261

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247
ChainResidueDetails
CHIS297
ASER392
AGLU413
ATHR418
AASP491
ATYR503
ALYS512
ALYS612
BHIS297
BSER392
BGLU413
CSER392
BTHR418
BASP491
BTYR503
BLYS512
BLYS612
CGLU413
CTHR418
CASP491
CTYR503
CLYS512
CLYS612
AHIS297

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSO, ECO:0007744|PDB:5MSU
ChainResidueDetails
CTHR787
CTHR919
ATHR787
ATHR919
BTHR787
BTHR919

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSO, ECO:0007744|PDB:5MSU
ChainResidueDetails
CARG814
APRO880
ATYR956
ALYS960
BARG814
BARG824
BASP854
BPRO880
BTYR956
BLYS960
CARG824
CASP854
CPRO880
CTYR956
CLYS960
AARG814
AARG824
AASP854

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|HAMAP-Rule:MF_02247
ChainResidueDetails
CSER685
ASER685
BSER685

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PDB entries from 2024-11-13

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