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1N1D

Glycerol-3-phosphate cytidylyltransferase complexed with CDP-glycerol

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0009058biological_processbiosynthetic process
A0016779molecular_functionnucleotidyltransferase activity
A0019350biological_processteichoic acid biosynthetic process
A0046872molecular_functionmetal ion binding
A0047348molecular_functionglycerol-3-phosphate cytidylyltransferase activity
A0071555biological_processcell wall organization
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0009058biological_processbiosynthetic process
B0016779molecular_functionnucleotidyltransferase activity
B0019350biological_processteichoic acid biosynthetic process
B0046872molecular_functionmetal ion binding
B0047348molecular_functionglycerol-3-phosphate cytidylyltransferase activity
B0071555biological_processcell wall organization
C0003824molecular_functioncatalytic activity
C0005737cellular_componentcytoplasm
C0009058biological_processbiosynthetic process
C0016779molecular_functionnucleotidyltransferase activity
C0019350biological_processteichoic acid biosynthetic process
C0046872molecular_functionmetal ion binding
C0047348molecular_functionglycerol-3-phosphate cytidylyltransferase activity
C0071555biological_processcell wall organization
D0003824molecular_functioncatalytic activity
D0005737cellular_componentcytoplasm
D0009058biological_processbiosynthetic process
D0016779molecular_functionnucleotidyltransferase activity
D0019350biological_processteichoic acid biosynthetic process
D0046872molecular_functionmetal ion binding
D0047348molecular_functionglycerol-3-phosphate cytidylyltransferase activity
D0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
AHIS14
AHIS17
AARG113
ASER118
ATHR119
AC2G130
AHOH909

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 D 702
ChainResidue
DTHR119
DTHR120
DC2G430
DHOH820
DHOH881
DARG113
DSER118

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 705
ChainResidue
BHIS14
BHIS17
BSER118
BTHR119
BC2G230
BHOH780

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE C2G A 130
ChainResidue
AGLY8
ATHR9
APHE10
AHIS17
ASER36
ALYS44
ALYS46
AGLU71
ALYS77
AMET91
AGLY92
AASP94
ATRP95
AARG113
ATHR114
AILE117
ASO4701
AHOH721
AHOH733
AHOH745
AHOH845

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE C2G B 230
ChainResidue
BGLY8
BTHR9
BPHE10
BSER36
BLYS44
BLYS46
BGLU71
BTRP74
BLYS77
BGLY92
BASP94
BTRP95
BPHE99
BARG113
BTHR114
BILE117
BSO4705
BHOH707
BHOH740
BHOH748
BHOH780

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE C2G C 330
ChainResidue
CTYR7
CGLY8
CTHR9
CPHE10
CHIS17
CSER36
CLYS44
CLYS46
CGLU71
CLYS77
CMET91
CGLY92
CASP94
CTRP95
CARG113
CTHR114
CILE117
CHOH710
CHOH760
CHOH839

site_idAC7
Number of Residues22
DetailsBINDING SITE FOR RESIDUE C2G D 430
ChainResidue
DHOH723
DHOH739
DHOH812
DHOH820
DHOH892
DGLY8
DTHR9
DPHE10
DSER36
DLYS44
DLYS46
DGLU71
DLYS77
DMET91
DGLY92
DASP94
DTRP95
DARG113
DTHR114
DILE117
DSO4702
DHOH722

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:10508782, ECO:0000269|PubMed:14506262
ChainResidueDetails
ATHR9
CHIS14
CLYS46
CARG113
DTHR9
DHIS14
DLYS46
DARG113
AHIS14
ALYS46
AARG113
BTHR9
BHIS14
BLYS46
BARG113
CTHR9

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:14506262
ChainResidueDetails
ALYS44
ALYS77
BLYS44
BLYS77
CLYS44
CLYS77
DLYS44
DLYS77

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 296
ChainResidueDetails
ALYS44attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
ALYS46attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 296
ChainResidueDetails
BLYS44attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
BLYS46attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor

site_idMCSA3
Number of Residues2
DetailsM-CSA 296
ChainResidueDetails
CLYS44attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
CLYS46attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor

site_idMCSA4
Number of Residues2
DetailsM-CSA 296
ChainResidueDetails
DLYS44attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
DLYS46attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-07-24

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