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

6NKA

Crystal structure of Mycobacterium tuberculosis dethiobiotin synthetase in complex with 2'-deoxycytidine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004141molecular_functiondethiobiotin synthase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009102biological_processbiotin biosynthetic process
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004141molecular_functiondethiobiotin synthase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009102biological_processbiotin biosynthetic process
B0016874molecular_functionligase activity
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004141molecular_functiondethiobiotin synthase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0009102biological_processbiotin biosynthetic process
C0016874molecular_functionligase activity
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0004141molecular_functiondethiobiotin synthase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0009102biological_processbiotin biosynthetic process
D0016874molecular_functionligase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue SO4 A 301
ChainResidue
AGLY12
AVAL13
AGLY14
ALYS15
ATHR16
ADCZ302
AHOH436
AHOH451
AHOH491

site_idAC2
Number of Residues7
Detailsbinding site for residue DCZ A 302
ChainResidue
AGLY169
APRO197
AGLY199
AALA200
AALA201
ASO4301
AHOH402

site_idAC3
Number of Residues11
Detailsbinding site for residue SO4 B 301
ChainResidue
BGLY12
BVAL13
BGLY14
BLYS15
BTHR16
BDCZ302
BHOH405
BHOH412
BHOH452
BHOH487
BHOH492

site_idAC4
Number of Residues10
Detailsbinding site for residue DCZ B 302
ChainResidue
BGLY12
BGLY169
BLEU196
BPRO197
BGLY199
BALA200
BALA201
BSO4301
BHOH429
BHOH483

site_idAC5
Number of Residues8
Detailsbinding site for residue SO4 C 301
ChainResidue
CGLY12
CVAL13
CGLY14
CLYS15
CTHR16
CDCZ302
CHOH401
CHOH465

site_idAC6
Number of Residues9
Detailsbinding site for residue DCZ C 302
ChainResidue
CGLY169
CLEU196
CPRO197
CGLY199
CALA200
CALA201
CSO4301
CHOH407
CHOH409

site_idAC7
Number of Residues10
Detailsbinding site for residue SO4 D 301
ChainResidue
DGLY12
DVAL13
DGLY14
DLYS15
DTHR16
DDCZ302
DHOH412
DHOH416
DHOH419
DHOH422

site_idAC8
Number of Residues10
Detailsbinding site for residue DCZ D 302
ChainResidue
DGLY12
DVAL17
DGLY169
DLEU196
DPRO197
DGLY199
DALA200
DALA201
DSO4301
DHOH418

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00336
ChainResidueDetails
ALYS37
BLYS37
CLYS37
DLYS37

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:25801336, ECO:0000269|PubMed:30289406, ECO:0000269|DOI:10.1021/acscatal.8b03475, ECO:0007744|PDB:4WOP, ECO:0007744|PDB:6CVE, ECO:0007744|PDB:6CVF, ECO:0007744|PDB:6E05, ECO:0007744|PDB:6E06
ChainResidueDetails
ATHR11
APRO197
BTHR11
BPRO197
CTHR11
CPRO197
DTHR11
DPRO197

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00336, ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:30289406, ECO:0000269|DOI:10.1021/acscatal.8b03475, ECO:0007744|PDB:3FPA, ECO:0007744|PDB:6CVE, ECO:0007744|PDB:6CVF, ECO:0007744|PDB:6CVV, ECO:0007744|PDB:6CZB, ECO:0007744|PDB:6CZC, ECO:0007744|PDB:6CZD, ECO:0007744|PDB:6CZE, ECO:0007744|PDB:6E05, ECO:0007744|PDB:6E06
ChainResidueDetails
ATHR16
DTHR16
DASP49
DGLU108
AASP49
AGLU108
BTHR16
BASP49
BGLU108
CTHR16
CASP49
CGLU108

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20565114, ECO:0000269|DOI:10.1021/acscatal.8b03475, ECO:0007744|PDB:3FMF, ECO:0007744|PDB:3FMI, ECO:0007744|PDB:6CVE
ChainResidueDetails
ALYS37
BLYS37
CLYS37
DLYS37

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00336
ChainResidueDetails
ATHR41
BTHR41
CTHR41
DTHR41

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20565114, ECO:0000269|DOI:10.1021/acscatal.8b03475, ECO:0007744|PDB:3FMF, ECO:0007744|PDB:3FMI, ECO:0007744|PDB:3FPA, ECO:0007744|PDB:6CVE
ChainResidueDetails
AGLY144
BGLY144
CGLY144
DGLY144

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:30289406, ECO:0000269|DOI:10.1021/acscatal.8b03475, ECO:0007744|PDB:6CVE, ECO:0007744|PDB:6CVF, ECO:0007744|PDB:6CVU, ECO:0007744|PDB:6E05, ECO:0007744|PDB:6E06
ChainResidueDetails
AGLY169
BGLY169
CGLY169
DGLY169

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon