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

4MVD

Crystal Structure of a Mammalian Cytidylyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004105molecular_functioncholine-phosphate cytidylyltransferase activity
A0006657biological_processCDP-choline pathway
A0009058biological_processbiosynthetic process
B0003824molecular_functioncatalytic activity
B0004105molecular_functioncholine-phosphate cytidylyltransferase activity
B0006657biological_processCDP-choline pathway
B0009058biological_processbiosynthetic process
C0003824molecular_functioncatalytic activity
C0004105molecular_functioncholine-phosphate cytidylyltransferase activity
C0006657biological_processCDP-choline pathway
C0009058biological_processbiosynthetic process
D0003824molecular_functioncatalytic activity
D0004105molecular_functioncholine-phosphate cytidylyltransferase activity
D0006657biological_processCDP-choline pathway
D0009058biological_processbiosynthetic process
E0003824molecular_functioncatalytic activity
E0004105molecular_functioncholine-phosphate cytidylyltransferase activity
E0006657biological_processCDP-choline pathway
E0009058biological_processbiosynthetic process
F0003824molecular_functioncatalytic activity
F0004105molecular_functioncholine-phosphate cytidylyltransferase activity
F0006657biological_processCDP-choline pathway
F0009058biological_processbiosynthetic process
G0003824molecular_functioncatalytic activity
G0004105molecular_functioncholine-phosphate cytidylyltransferase activity
G0006657biological_processCDP-choline pathway
G0009058biological_processbiosynthetic process
H0003824molecular_functioncatalytic activity
H0004105molecular_functioncholine-phosphate cytidylyltransferase activity
H0006657biological_processCDP-choline pathway
H0009058biological_processbiosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CDC B 401
ChainResidue
BASP82
BARG196
BTHR197
BILE200
BGLY83
BILE84
BPHE85
BALA95
BPRO150
BTRP151
BASP169
BGLN195

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CDC A 401
ChainResidue
AASP82
AGLY83
AILE84
APHE85
AGLY91
AALA95
ATRP151
AASP169
AGLN195
AARG196
ATHR197
AILE200

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CDC D 401
ChainResidue
DASP82
DGLY83
DILE84
DPHE85
DALA95
DPRO150
DTRP151
DASP169
DGLN195
DARG196
DTHR197
DILE200

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CDC C 401
ChainResidue
CASP82
CGLY83
CILE84
CPHE85
CGLY91
CALA95
CTRP151
CASP169
CGLN195
CARG196
CTHR197
CILE200

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CDC F 401
ChainResidue
FASP82
FGLY83
FILE84
FPHE85
FALA95
FPRO150
FTRP151
FASP169
FGLN195
FARG196
FTHR197
FILE200

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CDC E 401
ChainResidue
EASP82
EGLY83
EILE84
EPHE85
EGLY91
EALA95
ETRP151
EASP169
EGLN195
EARG196
ETHR197
EILE200

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CDC H 401
ChainResidue
HASP82
HGLY83
HILE84
HPHE85
HALA95
HPRO150
HTRP151
HASP169
HGLN195
HARG196
HTHR197
HILE200

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CDC G 401
ChainResidue
GASP82
GGLY83
GILE84
GPHE85
GGLY91
GALA95
GTRP151
GASP169
GGLN195
GARG196
GTHR197
GILE200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:19783652, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC, ECO:0007744|PDB:4MVD
ChainResidueDetails
BILE84
FARG196
EILE84
EARG196
HILE84
HARG196
GILE84
GARG196
BARG196
AILE84
AARG196
DILE84
DARG196
CILE84
CARG196
FILE84

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:19783652, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC
ChainResidueDetails
BLYS122
CLYS122
CHIS168
CTYR173
FLYS122
FHIS168
FTYR173
ELYS122
EHIS168
ETYR173
HLYS122
BHIS168
HHIS168
HTYR173
GLYS122
GHIS168
GTYR173
BTYR173
ALYS122
AHIS168
ATYR173
DLYS122
DHIS168
DTYR173

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19783652, ECO:0007744|PDB:3HL4
ChainResidueDetails
BTRP151
ATRP151
DTRP151
CTRP151
FTRP151
ETRP151
HTRP151
GTRP151

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P49585
ChainResidueDetails
BMET1
AMET1
DMET1
CMET1
FMET1
EMET1
HMET1
GMET1

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P49585
ChainResidueDetails
BLYS8
ALYS8
DLYS8
CLYS8
FLYS8
ELYS8
HLYS8
GLYS8

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49585
ChainResidueDetails
BSER233
ASER233
DSER233
CSER233
FSER233
ESER233
HSER233
GSER233

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon