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6EX8

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 Residues23
Detailsbinding site for residue C2K A 301
ChainResidue
AARG8
ALEU45
APHE61
AGLY64
AGLY65
AGLY66
ALEU67
AMET68
AASN70
AALA138
ALEU160
AGLU9
AASP161
AHIS162
AEDO307
AHOH458
AVAL13
APRO15
AGLN19
AGLY23
ASER24
ACSX25
ATRP26

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 302
ChainResidue
AGLY42
AASN43
APRO44
AASN73
AASN77
AHOH467

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 304
ChainResidue
ATHR58
ATRP74
ASER78
AHOH418
BTHR153
BSER154
BEDO301

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 305
ChainResidue
AARG195
AHOH421
AHOH531

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO A 306
ChainResidue
ASER78
AASN79
AGLY80
AHOH445
AHOH503
BTHR142
BTHR156

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO A 307
ChainResidue
AVAL13
ATHR14
APRO15
AC2K301
AHOH401
AHOH408

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO B 301
ChainResidue
AEDO304
BGLY149
BHOH485

site_idAC8
Number of Residues6
Detailsbinding site for residue EDO B 302
ChainResidue
BGLY80
BASN82
BALA111
BILE112
BHOH404
BHOH435

site_idAC9
Number of Residues6
Detailsbinding site for residue EDO B 303
ChainResidue
BPRO44
BILE59
BASN73
BTRP74
BASN77
BSER78

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO B 304
ChainResidue
AGLU97
BSER55
BASP57
BASP60
BGLN98

site_idAD2
Number of Residues24
Detailsbinding site for residue C2K B 305
ChainResidue
BARG8
BGLU9
BVAL13
BPRO15
BGLN19
BGLY23
BSER24
BCSX25
BTRP26
BLEU45
BPHE61
BGLY64
BGLY65
BGLY66
BLEU67
BMET68
BASN70
BALA138
BLEU160
BASP161
BEDO312
BHOH401
BHOH463
BHOH526

site_idAD3
Number of Residues6
Detailsbinding site for residue EDO B 306
ChainResidue
BGLY20
BTRP184
BHOH421
AASN186
AMET187
BASP18

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO B 307
ChainResidue
BTRP38
BALA110
BEDO310

site_idAD5
Number of Residues7
Detailsbinding site for residue EDO B 308
ChainResidue
AASP18
AGLY20
AGLY94
BVAL16
BSER185
BASN186
BHOH426

site_idAD6
Number of Residues2
Detailsbinding site for residue EDO B 309
ChainResidue
APRO119
AGLN120

site_idAD7
Number of Residues9
Detailsbinding site for residue EDO B 310
ChainResidue
BTRP38
BVAL214
BGLY215
BGLY216
BPRO217
BEDO307
BHOH405
BHOH419
BHOH448

site_idAD8
Number of Residues4
Detailsbinding site for residue EDO B 311
ChainResidue
BALA141
BASP161
BHIS162
BHOH412

site_idAD9
Number of Residues6
Detailsbinding site for residue EDO B 312
ChainResidue
BARG8
BVAL13
BTHR14
BC2K305
BHOH402
BHOH409

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 2024-09-11

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