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6B5K

Mycobacterium tuberculosis RmlA in complex with Mg/dTTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005886cellular_componentplasma membrane
A0006006biological_processglucose metabolic process
A0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
A0009058biological_processbiosynthetic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016779molecular_functionnucleotidyltransferase activity
A0019305biological_processdTDP-rhamnose biosynthetic process
A0045226biological_processextracellular polysaccharide biosynthetic process
A0046075biological_processdTTP metabolic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0005886cellular_componentplasma membrane
B0006006biological_processglucose metabolic process
B0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
B0009058biological_processbiosynthetic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0016779molecular_functionnucleotidyltransferase activity
B0019305biological_processdTDP-rhamnose biosynthetic process
B0045226biological_processextracellular polysaccharide biosynthetic process
B0046075biological_processdTTP metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues31
Detailsbinding site for residue TTP A 301
ChainResidue
ALEU6
AGLN24
AGLN80
APRO83
AASP84
AGLY85
ALEU86
AGLY107
AASP108
AGLU193
AMG302
AALA7
AMG303
AHOH425
AHOH434
AHOH463
AHOH471
AHOH474
AHOH483
AHOH484
AHOH486
AHOH513
AGLY8
AHOH528
AHOH536
AGLY9
ASER10
AGLY11
ATHR12
AARG13
ALYS23

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 302
ChainResidue
AASP108
AASP222
ATTP301
AHOH425
AHOH483
AHOH528

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 303
ChainResidue
ATTP301
AHOH463
AHOH474
AHOH536

site_idAC4
Number of Residues12
Detailsbinding site for residue TYD A 304
ChainResidue
AMET43
ATYR112
AGLY113
APRO114
AGLY115
AGLY117
ATHR118
ASER119
AVAL247
ASER248
AGLU252
AHOH430

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 305
ChainResidue
AARG122
ASER125
AHOH450
AHOH466
AHOH529

site_idAC6
Number of Residues4
Detailsbinding site for residue MG B 301
ChainResidue
BTTP303
BHOH435
BHOH462
BHOH481

site_idAC7
Number of Residues6
Detailsbinding site for residue MG B 302
ChainResidue
BASP108
BASP222
BTTP303
BHOH409
BHOH426
BHOH478

site_idAC8
Number of Residues29
Detailsbinding site for residue TTP B 303
ChainResidue
BLEU6
BGLY8
BGLY9
BSER10
BGLY11
BTHR12
BARG13
BLYS23
BGLN24
BGLN80
BPRO83
BASP84
BGLY85
BLEU86
BGLY107
BASP108
BGLU193
BMG301
BMG302
BHOH409
BHOH417
BHOH426
BHOH435
BHOH436
BHOH449
BHOH462
BHOH476
BHOH478
BHOH481

site_idAC9
Number of Residues13
Detailsbinding site for residue TYD B 304
ChainResidue
BGLY113
BGLY115
BGLY117
BTHR118
BSER119
BVAL247
BSER248
BGLU252
BARG256
BHOH464
BHOH475
BMET43
BTYR112

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:29076563, ECO:0007744|PDB:6B5K
ChainResidueDetails
ALYS23
AGLN24
AGLN80
AGLY85
BGLY8
BGLY11
BTHR12
BARG13
BLYS23
BGLN24
BGLN80
BGLY85
AGLY8
AGLY11
ATHR12
AARG13

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:29076563, ECO:0007744|PDB:6B5E, ECO:0007744|PDB:6B5K
ChainResidueDetails
AASP108
AASP222
BASP108
BASP222

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:29076563, ECO:0007744|PDB:6B5E
ChainResidueDetails
AASN109
AGLY143
AGLU158
ALYS159
AVAL169
BASN109
BGLY143
BGLU158
BLYS159
BVAL169

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphothreonine; by PknB => ECO:0000269|PubMed:33868202
ChainResidueDetails
ATHR12
ATHR54
ATHR197
BTHR12
BTHR54
BTHR197

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PDB entries from 2024-05-15

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