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

6W32

Crystal structure of Sfh5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000329cellular_componentfungal-type vacuole membrane
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006869biological_processlipid transport
A0008526molecular_functionphosphatidylinositol transfer activity
A0015914biological_processphospholipid transport
A0017157biological_processregulation of exocytosis
A0020037molecular_functionheme binding
A0032541cellular_componentcortical endoplasmic reticulum
A0043001biological_processGolgi to plasma membrane protein transport
A0046488biological_processphosphatidylinositol metabolic process
A0046872molecular_functionmetal ion binding
A0071944cellular_componentcell periphery
A0120009biological_processintermembrane lipid transfer
A2000114biological_processregulation of establishment of cell polarity
B0000329cellular_componentfungal-type vacuole membrane
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006869biological_processlipid transport
B0008526molecular_functionphosphatidylinositol transfer activity
B0015914biological_processphospholipid transport
B0017157biological_processregulation of exocytosis
B0020037molecular_functionheme binding
B0032541cellular_componentcortical endoplasmic reticulum
B0043001biological_processGolgi to plasma membrane protein transport
B0046488biological_processphosphatidylinositol metabolic process
B0046872molecular_functionmetal ion binding
B0071944cellular_componentcell periphery
B0120009biological_processintermembrane lipid transfer
B2000114biological_processregulation of establishment of cell polarity
C0000329cellular_componentfungal-type vacuole membrane
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005789cellular_componentendoplasmic reticulum membrane
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006869biological_processlipid transport
C0008526molecular_functionphosphatidylinositol transfer activity
C0015914biological_processphospholipid transport
C0017157biological_processregulation of exocytosis
C0020037molecular_functionheme binding
C0032541cellular_componentcortical endoplasmic reticulum
C0043001biological_processGolgi to plasma membrane protein transport
C0046488biological_processphosphatidylinositol metabolic process
C0046872molecular_functionmetal ion binding
C0071944cellular_componentcell periphery
C0120009biological_processintermembrane lipid transfer
C2000114biological_processregulation of establishment of cell polarity
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue HEM B 301
ChainResidue
BTYR128
BVAL194
BPHE198
BLYS209
BPHE211
BPHE218
BVAL221
BTYR222
BILE225
BVAL229
BPHE237
BPHE138
BARG148
BHIS173
BTYR175
BVAL178
BMET183
BILE187
BSER191

site_idAC2
Number of Residues17
Detailsbinding site for residue HEM A 301
ChainResidue
ATYR128
APHE138
APHE144
AARG148
AHIS173
ATYR175
AVAL178
AILE187
ASER191
AVAL194
AILE195
ALYS209
APHE211
APHE218
AVAL221
AILE225
AVAL229

site_idAC3
Number of Residues18
Detailsbinding site for residue HEM C 301
ChainResidue
CTYR128
CPHE138
CPHE144
CARG148
CHIS173
CTYR175
CVAL178
CILE187
CSER191
CVAL194
CILE195
CLYS209
CPHE211
CPHE218
CVAL221
CILE225
CVAL229
CPHE237

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues498
DetailsDomain: {"description":"CRAL-TRIO","evidences":[{"source":"PROSITE-ProRule","id":"PRU00056","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A6ZQI5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"UniProtKB","id":"A6ZQI5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

PDB statisticsPDBj update infoContact PDBjnumon