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

3TYI

Crystal Structure of Cytochrome c - p-Sulfonatocalix[4]arene Complexes

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
A0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A1901612molecular_functioncardiolipin binding
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005758cellular_componentmitochondrial intermembrane space
B0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
B0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B1901612molecular_functioncardiolipin binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 104
ChainResidue
AARG13
AGLY41
ATYR46
ATYR48
ATHR49
AASN52
ATRP59
AMET64
ATYR67
ATHR78
ALYS79
ACYS14
AMET80
APHE82
AHOH172
AHOH209
ACYS17
AHIS18
AVAL28
AGLY29
APRO30
AILE35
ASER40

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE T3Y A 105
ChainResidue
ALYS-2
ASER2
AALA3
ALYS4
ALYS5
AALA7
ALYS87
AGLU88
ALYS89
AASN92
ATYR97
ALYS100
AHOH109
AHOH121
AHOH124
AHOH125
AHOH132
AHOH142
AHOH149
AHOH186
AHOH201
AHOH206
AHOH223
AHOH229
AHOH236
AHOH316

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM B 104
ChainResidue
BARG13
BCYS14
BCYS17
BHIS18
BVAL28
BPRO30
BILE35
BSER40
BGLY41
BTYR46
BTYR48
BTHR49
BASN52
BTRP59
BMET64
BTYR67
BLEU68
BTHR78
BLYS79
BMET80
BALA81
BPHE82
BLEU94
BHOH160
BHOH181

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE T3Y B 105
ChainResidue
AASP50
ALYS54
BSER2
BALA3
BLYS4
BLYS5
BASN70
BLYS72
BLYS73
BPRO76
BHOH134
BHOH167
BHOH176
BHOH177
BHOH190
BHOH215
BHOH273
BHOH283
BHOH288
BHOH307
BHOH389

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE T3Y B 106
ChainResidue
BLYS79
BLYS87
BGLU88
BLYS89
BASN92
BGLU103
BHOH139
BHOH146
BHOH196
BHOH206
BHOH249
BHOH271
BHOH392
BLYS22
BGLY23
BVAL28
BHIS33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5
ChainResidueDetails
ACYS14
ACYS17
BCYS14
BCYS17

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5
ChainResidueDetails
AHIS18
AMET80
BHIS18
BMET80

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO
ChainResidueDetails
ALYS72
BLYS72

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544
ChainResidueDetails
ALYS73
BLYS73

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon