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

5V7P

Atomic structure of the eukaryotic intramembrane Ras methyltransferase ICMT (isoprenylcysteine carboxyl methyltransferase), in complex with a monobody

Functional Information from GO Data
ChainGOidnamespacecontents
A0004671molecular_functionprotein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006481biological_processC-terminal protein methylation
A0008168molecular_functionmethyltransferase activity
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue SAH A 301
ChainResidue
AASN183
AHIS209
APRO210
ASER211
ATYR212
AGLU250
ALEU254
AHOH413
AHOH415
AHOH427
APHE184
AASN185
AGLN189
AHIS196
AVAL197
ALEU198
AVAL199
ATYR204

site_idAC2
Number of Residues1
Detailsbinding site for residue UND A 302
ChainResidue
AILE112

site_idAC3
Number of Residues2
Detailsbinding site for residue UND A 303
ChainResidue
AMET25
AHIS28

site_idAC4
Number of Residues1
Detailsbinding site for residue D10 A 304
ChainResidue
ATYR217

site_idAC5
Number of Residues5
Detailsbinding site for residue D10 A 305
ChainResidue
ATYR217
ATHR271
AGLY272
AILE273
AILE276

site_idAC6
Number of Residues1
Detailsbinding site for residue D10 A 306
ChainResidue
DVAL1

site_idAC7
Number of Residues4
Detailsbinding site for residue D10 A 308
ChainResidue
ALEU71
AMET99
ATRP139
AD10310

site_idAC8
Number of Residues2
Detailsbinding site for residue UND A 309
ChainResidue
ASER137
AILE144

site_idAC9
Number of Residues4
Detailsbinding site for residue D10 A 310
ChainResidue
AILE81
AD10308
AD10311
AMPG323

site_idAD1
Number of Residues1
Detailsbinding site for residue D10 A 311
ChainResidue
AD10310

site_idAD2
Number of Residues1
Detailsbinding site for residue D10 A 312
ChainResidue
ATRP157

site_idAD3
Number of Residues2
Detailsbinding site for residue D10 A 313
ChainResidue
APHE148
APHE149

site_idAD4
Number of Residues2
Detailsbinding site for residue D10 A 314
ChainResidue
APHE70
ATYR131

site_idAD5
Number of Residues1
Detailsbinding site for residue D10 A 315
ChainResidue
AHIS127

site_idAD6
Number of Residues5
Detailsbinding site for residue MPG A 316
ChainResidue
ASER128
AVAL171
DTYR78
DTYR79
DHOH114

site_idAD7
Number of Residues5
Detailsbinding site for residue MPG A 317
ChainResidue
ALYS82
ALEU83
AGLN90
AHIS156
AASN160

site_idAD8
Number of Residues9
Detailsbinding site for residue MPG A 318
ChainResidue
APRO4
ALYS7
AILE8
AGLN11
APHE56
ATYR57
DALA12
DLEU19
DHOH124

site_idAD9
Number of Residues5
Detailsbinding site for residue MPG A 319
ChainResidue
AMPG321
DVAL1
DALA26
DVAL27
DTYR78

site_idAE1
Number of Residues7
Detailsbinding site for residue MPG A 320
ChainResidue
AGLY31
AILE32
ATHR33
AVAL37
APHE216
AILE220
ATRP240

site_idAE2
Number of Residues8
Detailsbinding site for residue MPG A 321
ChainResidue
ALEU178
ATHR179
AHIS201
AMPG319
AMPG322
DVAL1
DSER2
DSER3

site_idAE3
Number of Residues5
Detailsbinding site for residue MPG A 322
ChainResidue
ATYR30
ALEU237
AMET241
AMPG321
DPRO81

site_idAE4
Number of Residues5
Detailsbinding site for residue MPG A 323
ChainResidue
ATHR33
ATHR39
ATYR80
AVAL84
AD10310

site_idAE5
Number of Residues7
Detailsbinding site for residue MPG A 324
ChainResidue
AALA234
ALEU237
AILE23
APHE26
AASN27
ATYR45
APRO233

site_idAE6
Number of Residues11
Detailsbinding site for residue MPG A 325
ChainResidue
ATYR95
AMET99
AASN126
ATYR131
ATRP215
ASER219
ATHR222
AGLN223
ATYR235
ASER239
DTRP80

Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGNSP
ChainResidueDetails
DGLY37-PRO44

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:29342140
ChainResidueDetails
AMET1-LEU2
ALYS54-ASN58
AGLN114-VAL118
ASER182-ARG208
ALYS244-ILE281

site_idSWS_FT_FI2
Number of Residues178
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:29342140
ChainResidueDetails
ASER3-TYR29
AVAL36-LEU53
AGLU59-ALA85
AILE89-VAL113
ASER119-PHE149
AHIS156-GLY181
AHIS209-LEU226
ALEU230-PHE243

site_idSWS_FT_FI3
Number of Residues14
DetailsTOPO_DOM: Lumenal => ECO:0000305|PubMed:29342140
ChainResidueDetails
ATYR30-LEU35
APRO86-ASN88
APRO150-ILE155
AILE227-PRO229

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:29342140, ECO:0007744|PDB:5V7P, ECO:0007744|PDB:5VG9
ChainResidueDetails
AGLN189
AHIS196
ATYR204
AHIS209
AGLU250

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:29342140
ChainResidueDetails
AARG246

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon