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

6R29

Crystal structure of the SucA domain of Mycobacterium smegmatis KGD cocrystallized with succinylphosphonate

Functional Information from GO Data
ChainGOidnamespacecontents
A0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
A0030976molecular_functionthiamine pyrophosphate binding
B0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
B0030976molecular_functionthiamine pyrophosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues32
Detailsbinding site for residue QSP A 2001
ChainResidue
AHIS539
AALA646
AALA647
AGLN651
AASN678
AILE680
AGLY681
AHIS747
AMG2002
AHOH2130
AHOH2132
AARG540
AHOH2277
AHOH2288
AHOH2292
AHOH2431
AHOH2433
AHOH2496
BGLN901
BLEU950
BGLU952
BGLN976
ATYR578
BPHE977
BPHE980
BHIS1020
AHIS579
ASER604
AHIS605
ALEU606
AGLY644
AASP645

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 2002
ChainResidue
AASP645
AASN678
AILE680
AQSP2001
AHOH2288

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 2003
ChainResidue
AASP1004
AHIS1055
AASP1058
AILE1060
AHOH2493
AHOH2656

site_idAC4
Number of Residues6
Detailsbinding site for residue MPD A 2004
ChainResidue
AARG771
ALYS772
AGLU776
AGLU790
AGLU873
AHOH2173

site_idAC5
Number of Residues3
Detailsbinding site for residue MPD A 2005
ChainResidue
ATHR1183
AHOH2418
BPRO1178

site_idAC6
Number of Residues3
Detailsbinding site for residue MPD A 2006
ChainResidue
APHE424
AGLU468
AHOH2262

site_idAC7
Number of Residues32
Detailsbinding site for residue QSP B 2001
ChainResidue
AGLN901
ALEU950
AGLU952
AGLN976
APHE977
APHE980
AHIS1020
BHIS539
BARG540
BTYR578
BHIS579
BSER604
BHIS605
BLEU606
BGLY644
BASP645
BALA646
BALA647
BGLN651
BASN678
BILE680
BGLY681
BHIS747
BMG2002
BHOH2125
BHOH2180
BHOH2182
BHOH2272
BHOH2298
BHOH2366
BHOH2424
BHOH2439

site_idAC8
Number of Residues5
Detailsbinding site for residue MG B 2002
ChainResidue
BASP645
BASN678
BILE680
BQSP2001
BHOH2298

site_idAC9
Number of Residues6
Detailsbinding site for residue MG B 2003
ChainResidue
BASP1004
BHIS1055
BASP1058
BILE1060
BHOH2523
BHOH2553

site_idAD1
Number of Residues2
Detailsbinding site for residue MPD B 2004
ChainResidue
BHOH2495
BTHR1086

site_idAD2
Number of Residues4
Detailsbinding site for residue MPD B 2005
ChainResidue
AALA1172
APRO1178
BTHR1183
BHOH2446

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:21867916, ECO:0007744|PDB:2XTA
ChainResidueDetails
AARG540
AARG1054
ALYS1089
ASER1092
AGLN1142
AARG1149
AARG1150
BARG540
BSER604
BLEU606
BASP645
ASER604
BALA646
BALA647
BASN678
BILE680
BTHR1038
BARG1054
BLYS1089
BSER1092
BGLN1142
BARG1149
ALEU606
BARG1150
AASP645
AALA646
AALA647
AASN678
AILE680
ATHR1038

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:21867916, ECO:0007744|PDB:2Y0P
ChainResidueDetails
AHIS579
AHIS1020
BHIS579
BHIS1020

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon