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6EXQ

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 Residues2
Detailsbinding site for residue EDO A 301
ChainResidue
AMET145
AASP161

site_idAC2
Number of Residues15
Detailsbinding site for residue C2W A 302
ChainResidue
AGLY65
AGLY66
ALEU67
AMET68
AALA138
ALEU160
AASP161
AHIS162
AARG8
AVAL13
AGLY23
ACYS25
AASP60
APHE61
AGLY64

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 303
ChainResidue
APRO119
AGLN120
BALA1
BGLU131

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO B 301
ChainResidue
BALA4
BGLU9
BGLN207

site_idAC5
Number of Residues8
Detailsbinding site for residue EDO B 302
ChainResidue
BASP6
BARG8
BGLU9
BGLN159
BLEU160
BGLN207
BC2W303
BHOH405

site_idAC6
Number of Residues18
Detailsbinding site for residue C2W B 303
ChainResidue
BARG8
BVAL13
BGLY23
BCYS25
BTRP26
BPHE61
BGLY64
BGLY65
BGLY66
BLEU67
BMET68
BASN70
BALA138
BLEU160
BASP161
BEDO302
BHOH405
BHOH438

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO B 304
ChainResidue
BPRO2
BALA3

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

223532

PDB entries from 2024-08-07

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