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4MVC

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
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE CDC A 401
ChainResidue
AASP82
AHIS168
AASP169
ATYR173
ATYR182
AGLN195
AARG196
ATHR197
AILE200
AHOH504
AGLY83
AILE84
APHE85
AHIS89
AGLY91
AALA95
ALYS122
ATRP151

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE CDC B 401
ChainResidue
BASP82
BGLY83
BILE84
BPHE85
BHIS89
BGLY91
BHIS92
BALA95
BLYS122
BPRO150
BTRP151
BHIS168
BASP169
BTYR173
BTYR182
BGLN195
BARG196
BTHR197
BILE200
BHOH502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:19783652, ECO:0000305|PubMed:24275660, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC, ECO:0007744|PDB:4MVD
ChainResidueDetails
AILE84
BARG196
BTHR197
BILE200
APHE85
AGLN195
AARG196
ATHR197
AILE200
BILE84
BPHE85
BGLN195

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19783652, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC, ECO:0007744|PDB:4MVD
ChainResidueDetails
AHIS92
BHIS92

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:19783652, ECO:0000305|PubMed:24275660, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC
ChainResidueDetails
ALYS122
AHIS168
AASP169
ATYR173
BLYS122
BHIS168
BASP169
BTYR173

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:19783652, ECO:0000305|PubMed:24275660, ECO:0007744|PDB:3HL4
ChainResidueDetails
ATRP151
BTRP151

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P49585
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P49585
ChainResidueDetails
ALYS8
BLYS8

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49585
ChainResidueDetails
ASER265
BSER265

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PDB entries from 2024-10-30

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