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6EXO

Crystal Structure of Rhodesain in complex with a Macrolactam Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EDO A 301
ChainResidue
ATHR58
ATRP74
ASER78
BTHR153
BSER154
BEDO306

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 302
ChainResidue
AASN73
AASN77
AHOH406
AGLY42
AASN43
APRO44

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 303
ChainResidue
AGLU86
APRO90
ATYR91
BTYR91
BVAL92
BEDO312

site_idAC4
Number of Residues15
Detailsbinding site for residue C3E A 304
ChainResidue
AGLU9
AGLN19
AGLY23
ASER24
ACSX25
ATRP26
AGLY64
AGLY65
AGLY66
ALEU67
AMET68
AALA138
ALEU160
AASP161
AHIS162

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 305
ChainResidue
AASP114
AVAL213

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 306
ChainResidue
AASP69
AASN73
AHIS115
AASP117
AHOH507

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 307
ChainResidue
ATRP38
APRO44
AVAL46
AHOH485

site_idAC8
Number of Residues6
Detailsbinding site for residue EDO A 308
ChainResidue
AASP18
AGLN19
AGLY20
AEDO309
BASN186
BMET187

site_idAC9
Number of Residues9
Detailsbinding site for residue EDO A 309
ChainResidue
AASP18
AGLY20
AGLY94
AEDO308
BVAL16
BSER185
BASN186
BEDO311
BHOH408

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO A 310
ChainResidue
ATYR89
APRO90
AVAL92
APRO99
AHOH401

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO A 311
ChainResidue
AGLY80
AALA111
AILE112
ATHR113
AHOH450

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO A 312
ChainResidue
AARG195
AHOH436
AHOH480

site_idAD4
Number of Residues1
Detailsbinding site for residue EDO B 301
ChainResidue
BILE108

site_idAD5
Number of Residues8
Detailsbinding site for residue EDO B 302
ChainResidue
APRO119
BALA41
BASN43
BVAL214
BGLY215
BEDO309
BHOH425
BHOH455

site_idAD6
Number of Residues14
Detailsbinding site for residue C3E B 303
ChainResidue
BARG8
BGLN19
BGLY23
BCSX25
BTRP26
BGLY65
BGLY66
BLEU67
BMET68
BALA138
BLEU160
BASP161
BHOH445
BHOH499

site_idAD7
Number of Residues3
Detailsbinding site for residue EDO B 304
ChainResidue
BLYS10
BASP117
BGLN207

site_idAD8
Number of Residues8
Detailsbinding site for residue EDO B 305
ChainResidue
AMET187
BASP18
BGLN19
BGLY20
BTRP184
BEDO307
BHOH432
AASN186

site_idAD9
Number of Residues6
Detailsbinding site for residue EDO B 306
ChainResidue
AEDO301
BSER143
BASP146
BLEU152
BHOH405
BHOH414

site_idAE1
Number of Residues4
Detailsbinding site for residue EDO B 307
ChainResidue
BMET145
BTRP184
BEDO305
BHOH445

site_idAE2
Number of Residues3
Detailsbinding site for residue EDO B 308
ChainResidue
BASN79
BGLY80
BASN82

site_idAE3
Number of Residues4
Detailsbinding site for residue EDO B 309
ChainResidue
BALA41
BGLY42
BASN43
BEDO302

site_idAE4
Number of Residues6
Detailsbinding site for residue EDO B 310
ChainResidue
ASER78
AASN79
AGLY80
BSER143
BASP146
BTHR156

site_idAE5
Number of Residues5
Detailsbinding site for residue EDO B 311
ChainResidue
AEDO309
BLYS17
BASP18
BEDO313
BHOH410

site_idAE6
Number of Residues5
Detailsbinding site for residue EDO B 312
ChainResidue
ASER47
AALA87
AEDO303
BASN95
BGLU97

site_idAE7
Number of Residues7
Detailsbinding site for residue EDO B 313
ChainResidue
AASP18
BASP18
BGLY20
BTYR91
BGLY94
BEDO311
BHOH408

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfST
ChainResidueDetails
AGLN19-THR30

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. LDHGVLLVGYN
ChainResidueDetails
ALEU160-ASN170

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIiKNSWsnmWGedGYIrI
ChainResidueDetails
ATYR177-ILE196

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PDB entries from 2024-10-09

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