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

6JIL

Crystal structure of D-cycloserine synthetase DcsG

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0016874molecular_functionligase activity
A0016882molecular_functioncyclo-ligase activity
A0017000biological_processantibiotic biosynthetic process
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0016874molecular_functionligase activity
B0016882molecular_functioncyclo-ligase activity
B0017000biological_processantibiotic biosynthetic process
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0005524molecular_functionATP binding
C0016874molecular_functionligase activity
C0016882molecular_functioncyclo-ligase activity
C0017000biological_processantibiotic biosynthetic process
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0005524molecular_functionATP binding
D0016874molecular_functionligase activity
D0016882molecular_functioncyclo-ligase activity
D0017000biological_processantibiotic biosynthetic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue TLA A 401
ChainResidue
ATRP45
APHE69
AARG72
AVAL73
AHOH553

site_idAC2
Number of Residues13
Detailsbinding site for residue TLA A 402
ChainResidue
AARG254
AGLU269
AGLU271
ASER276
AADP403
AMG404
AMG405
AHOH528
AHOH584
ACYS142
ATYR143
ALYS202
AARG220

site_idAC3
Number of Residues23
Detailsbinding site for residue ADP A 403
ChainResidue
ALYS92
ALYS137
ACYS142
ATYR143
ASER144
AGLN175
APRO176
ATYR177
AVAL178
AGLU186
AMSE205
ALEU206
ALEU268
AGLU269
ATLA402
AMG404
AMG405
AHOH516
AHOH526
AHOH527
AHOH535
AHOH554
AHOH592

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 404
ChainResidue
ALYS202
AGLU269
ATLA402
AADP403
AHOH501
AHOH527

site_idAC5
Number of Residues5
Detailsbinding site for residue MG A 405
ChainResidue
AGLU269
AGLU271
ATLA402
AADP403
AHOH526

site_idAC6
Number of Residues8
Detailsbinding site for residue TLA B 401
ChainResidue
BGLY114
BSER115
BALA117
BALA163
BLEU166
BALA167
BHOH505
BHOH515

site_idAC7
Number of Residues4
Detailsbinding site for residue TLA B 402
ChainResidue
BTRP45
BPHE69
BARG72
BVAL73

site_idAC8
Number of Residues14
Detailsbinding site for residue TLA B 403
ChainResidue
BCYS142
BTYR143
BLYS202
BARG220
BARG254
BGLU269
BGLU271
BSER276
BADP404
BMG405
BMG406
BHOH512
BHOH538
BHOH570

site_idAC9
Number of Residues25
Detailsbinding site for residue ADP B 404
ChainResidue
BHOH521
BHOH529
BHOH580
BHOH583
BLYS92
BVAL135
BLYS137
BGLY141
BCYS142
BTYR143
BSER144
BGLN175
BPRO176
BTYR177
BVAL178
BVAL181
BGLU186
BMSE205
BLEU206
BLEU268
BGLU269
BTLA403
BMG405
BMG406
BHOH512

site_idAD1
Number of Residues7
Detailsbinding site for residue MG B 405
ChainResidue
BLYS202
BASP256
BGLU269
BTLA403
BADP404
BHOH504
BHOH512

site_idAD2
Number of Residues5
Detailsbinding site for residue MG B 406
ChainResidue
BGLU269
BGLU271
BTLA403
BADP404
BHOH521

site_idAD3
Number of Residues7
Detailsbinding site for residue TLA C 401
ChainResidue
CGLY114
CSER115
CALA117
CLEU166
DGLU227
DASP228
DHOH558

site_idAD4
Number of Residues6
Detailsbinding site for residue TLA C 402
ChainResidue
CTRP45
CPHE69
CARG72
CVAL73
CVAL76
CHOH537

site_idAD5
Number of Residues12
Detailsbinding site for residue TLA C 403
ChainResidue
CCYS142
CTYR143
CLYS202
CARG220
CARG254
CGLU269
CGLU271
CSER276
CADP404
CMG405
CMG406
CHOH529

site_idAD6
Number of Residues23
Detailsbinding site for residue ADP C 404
ChainResidue
CLYS92
CLYS137
CCYS142
CTYR143
CSER144
CGLN175
CPRO176
CTYR177
CVAL178
CVAL181
CGLU186
CMSE205
CLEU206
CLEU268
CGLU269
CTLA403
CMG405
CMG406
CHOH510
CHOH536
CHOH540
CHOH548
CHOH562

site_idAD7
Number of Residues6
Detailsbinding site for residue MG C 405
ChainResidue
CLYS202
CGLU269
CTLA403
CADP404
CHOH501
CHOH570

site_idAD8
Number of Residues5
Detailsbinding site for residue MG C 406
ChainResidue
CGLU269
CGLU271
CTLA403
CADP404
CHOH562

site_idAD9
Number of Residues3
Detailsbinding site for residue TLA D 401
ChainResidue
DTRP45
DPHE69
DARG72

site_idAE1
Number of Residues14
Detailsbinding site for residue TLA D 402
ChainResidue
DTRP57
DCYS142
DTYR143
DLYS202
DPRO215
DARG254
DGLU269
DGLU271
DSER276
DADP403
DMG404
DMG405
DMG406
DHOH555

site_idAE2
Number of Residues24
Detailsbinding site for residue ADP D 403
ChainResidue
DLYS92
DVAL135
DLYS137
DCYS142
DTYR143
DSER144
DGLN175
DPRO176
DTYR177
DVAL178
DVAL181
DGLU186
DMSE205
DLEU206
DLEU268
DGLU269
DTLA402
DMG404
DMG405
DHOH502
DHOH512
DHOH538
DHOH542
DHOH543

site_idAE3
Number of Residues7
Detailsbinding site for residue MG D 404
ChainResidue
DLYS202
DASP256
DGLU269
DTLA402
DADP403
DHOH502
DHOH505

site_idAE4
Number of Residues6
Detailsbinding site for residue MG D 405
ChainResidue
DGLY141
DCYS142
DGLU269
DGLU271
DTLA402
DADP403

site_idAE5
Number of Residues4
Detailsbinding site for residue MG D 406
ChainResidue
DTRP57
DGLU271
DGLU274
DTLA402

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:31793174
ChainResidueDetails
AARG254
AGLU271
BARG220
BARG254
BGLU271
CARG220
CARG254
CGLU271
DARG220
DARG254
DGLU271
AARG220

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:31793174, ECO:0000312|PDB:6JIL
ChainResidueDetails
ALYS92
ALYS137
ASER144
AGLN175
APRO176
AVAL178
AGLU269
AGLU271
BLYS92
BLYS137
BSER144
BGLN175
BPRO176
BVAL178
BGLU269
BGLU271
CLYS92
CLYS137
CSER144
CGLN175
CPRO176
CVAL178
CGLU269
CGLU271
DLYS92
DLYS137
DSER144
DGLN175
DPRO176
DVAL178
DGLU269
DGLU271

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon