Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5DIR

membrane protein at 2.8 Angstroms

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004190molecular_functionaspartic-type endopeptidase activity
A0005886cellular_componentplasma membrane
A0006465biological_processsignal peptide processing
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
B0004175molecular_functionendopeptidase activity
B0004190molecular_functionaspartic-type endopeptidase activity
B0005886cellular_componentplasma membrane
B0006465biological_processsignal peptide processing
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
C0004175molecular_functionendopeptidase activity
C0004190molecular_functionaspartic-type endopeptidase activity
C0005886cellular_componentplasma membrane
C0006465biological_processsignal peptide processing
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
D0004175molecular_functionendopeptidase activity
D0004190molecular_functionaspartic-type endopeptidase activity
D0005886cellular_componentplasma membrane
D0006465biological_processsignal peptide processing
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue OLC A 201
ChainResidue
AILE100
APHE139
AASP143
ATHR147
AVAL148
AOLC204
ESER203
EALO204

site_idAC2
Number of Residues7
Detailsbinding site for residue OLC A 202
ChainResidue
APHE29
AGLU33
AILE40
ATRP49
ALEU141
AOLC203
ASER26

site_idAC3
Number of Residues3
Detailsbinding site for residue OLC A 203
ChainResidue
AVAL41
ATRP49
AOLC202

site_idAC4
Number of Residues9
Detailsbinding site for residue OLC A 204
ChainResidue
AVAL4
AGLY8
APRO11
ATRP12
AILE15
ALYS93
AOLC201
DVAL25
DALA32

site_idAC5
Number of Residues6
Detailsbinding site for residue OLC A 205
ChainResidue
ALEU10
APRO11
ATRP14
APHE20
DGLN31
DTYR114

site_idAC6
Number of Residues5
Detailsbinding site for residue OLC A 206
ChainResidue
APHE20
AARG70
AMET117
BVAL42
BOLC206

site_idAC7
Number of Residues10
Detailsbinding site for residue OLC B 201
ChainResidue
BTHR55
BPHE136
BPRO137
BALA138
BPHE139
BVAL148
BOLC202
BOLC203
HIIL202
HALO204

site_idAC8
Number of Residues5
Detailsbinding site for residue OLC B 202
ChainResidue
BPHE136
BTHR147
BVAL151
BALA154
BOLC201

site_idAC9
Number of Residues5
Detailsbinding site for residue OLC B 203
ChainResidue
BILE40
BVAL42
BTRP49
BOLC201
BOLC207

site_idAD1
Number of Residues7
Detailsbinding site for residue OLC B 204
ChainResidue
BGLY8
BARG9
BPRO11
BTRP12
BLYS93
BLEU104
CALA32

site_idAD2
Number of Residues6
Detailsbinding site for residue OLC B 205
ChainResidue
BPHE7
BTRP14
BVAL17
CTRP14
CALA28
CTYR114

site_idAD3
Number of Residues7
Detailsbinding site for residue OLC B 206
ChainResidue
AALA63
AASP64
ASER65
ATRP71
AOLC206
BTRP130
BTRP134

site_idAD4
Number of Residues6
Detailsbinding site for residue OLC B 207
ChainResidue
BLEU22
BSER26
BGLU33
BILE40
BTRP49
BOLC203

site_idAD5
Number of Residues3
Detailsbinding site for residue OLC C 201
ChainResidue
CVAL41
CVAL42
COLC204

site_idAD6
Number of Residues6
Detailsbinding site for residue OLC C 202
ChainResidue
CPHE20
CLEU110
CTYR114
CMET117
CVAL118
COLC203

site_idAD7
Number of Residues7
Detailsbinding site for residue OLC C 203
ChainResidue
DOLC205
CARG70
CILE78
CVAL85
CMET117
COLC202
DOLC204

site_idAD8
Number of Residues5
Detailsbinding site for residue OLC C 204
ChainResidue
CPHE29
CILE40
CTRP49
COLC201
FOLC301

site_idAD9
Number of Residues7
Detailsbinding site for residue OLC D 201
ChainResidue
DPHE136
DPHE139
DASP143
DTHR147
DVAL148
GSER203
GALO204

site_idAE1
Number of Residues6
Detailsbinding site for residue OLC D 202
ChainResidue
DLEU22
DGLU33
DILE40
DTRP49
DLEU141
DOLC203

site_idAE2
Number of Residues2
Detailsbinding site for residue OLC D 203
ChainResidue
DOLC202
DOLC204

site_idAE3
Number of Residues7
Detailsbinding site for residue OLC D 204
ChainResidue
CSER65
CTRP71
CMET117
COLC203
DTRP130
DOLC203
DOLC205

site_idAE4
Number of Residues4
Detailsbinding site for residue OLC D 205
ChainResidue
COLC203
DILE43
DTRP134
DOLC204

site_idAE5
Number of Residues9
Detailsbinding site for residue OLC F 301
ChainResidue
CVAL19
CPRO137
CPHE139
CASP143
CTHR147
CVAL148
COLC204
FSER203
FALO204

site_idAE6
Number of Residues3
Detailsbinding site for residue OLC F 302
ChainResidue
CLEU153
FALO204
F5BV205

site_idAE7
Number of Residues12
Detailsbinding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
ChainResidue
AASN54
APHE59
ALEU62
ALEU72
APHE73
AASN112
AARG116
AVAL122
AASP124
AASN140
AASP143
AOLC201

site_idAE8
Number of Residues12
Detailsbinding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
ChainResidue
CASN54
CGLY56
CPHE59
CPHE73
CASN112
CARG116
CVAL122
CASP124
CASN140
CASP143
FOLC301
FOLC302

site_idAE9
Number of Residues14
Detailsbinding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203
ChainResidue
DASN54
DALA57
DPHE59
DPHE73
DILE76
DALA77
DVAL80
DASN112
DARG116
DVAL122
DASP124
DASP143
DILE146
DOLC201

site_idAF1
Number of Residues12
Detailsbinding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
ChainResidue
BTHR55
BPHE73
BILE76
BALA77
BASN112
BARG116
BVAL122
BASP124
BASP143
BILE146
BTHR147
BOLC201

Functional Information from PROSITE/UniProt
site_idPS00855
Number of Residues13
DetailsSPASE_II Signal peptidases II signature. VlGGALGNLYDRM
ChainResidueDetails
AVAL105-MET117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00161","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26912896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30272004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DIR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FMS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues192
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"26912896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30272004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DIR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FMS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues168
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"26912896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30272004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DIR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FMS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues24
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26912896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30272004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DIR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FMS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues52
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"26912896","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DIR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00161","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26912896","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

PDB statisticsPDBj update infoContact PDBjnumon