Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6BGQ

Caspase-3 Mutant - S150D

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
C0004197molecular_functioncysteine-type endopeptidase activity
C0006508biological_processproteolysis
C0008234molecular_functioncysteine-type peptidase activity
D0004197molecular_functioncysteine-type endopeptidase activity
D0006508biological_processproteolysis
D0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CL A 301
ChainResidue
ALYS53
AGLY66
ATHR67
AASP68

site_idAC2
Number of Residues5
Detailsbinding site for residue AZI A 302
ChainResidue
AARG79
AASN80
ALYS82
AHOH415
DPHE252

site_idAC3
Number of Residues3
Detailsbinding site for residue AZI A 303
ChainResidue
ATHR92
AGLU94
AGLU95

site_idAC4
Number of Residues6
Detailsbinding site for residue AZI A 304
ChainResidue
ALYS137
ATHR140
AASN141
AARG144
BGLU190
BPHE193

site_idAC5
Number of Residues4
Detailsbinding site for residue AZI B 301
ChainResidue
BARG241
BHOH405
CASN35
DTHR270

site_idAC6
Number of Residues5
Detailsbinding site for residue AZI B 302
ChainResidue
BMET222
BGLN225
BTYR226
BARG238
BHOH445

site_idAC7
Number of Residues4
Detailsbinding site for residue CL C 201
ChainResidue
CLYS53
CGLY66
CTHR67
CASP68

site_idAC8
Number of Residues5
Detailsbinding site for residue AZI C 202
ChainResidue
BPHE252
CARG79
CASN80
CLYS82
CHOH437

site_idAC9
Number of Residues6
Detailsbinding site for residue AZI C 203
ChainResidue
CLYS137
CTHR140
CASN141
CARG144
DGLU190
DHOH404

site_idAD1
Number of Residues2
Detailsbinding site for residue AZI C 204
ChainResidue
CILE126
CTHR166

site_idAD2
Number of Residues3
Detailsbinding site for residue AZI C 205
ChainResidue
CTHR92
CGLU94
CASN131

site_idAD3
Number of Residues7
Detailsbinding site for residue NA D 301
ChainResidue
CTHR152
CGLY153
CLYS156
DILE187
DALA191
DASP192
DHOH427

site_idAD4
Number of Residues5
Detailsbinding site for residue AZI D 302
ChainResidue
AASN35
BTHR270
DARG238
DARG241
DHOH407

site_idAD5
Number of Residues17
Detailsbinding site for Ac-Asp-Glu-Val-Asp-CMK chain K
ChainResidue
ASER58
AARG64
AHIS121
AGLY122
AGLN161
ACYS163
BTYR204
BSER205
BTRP206
BARG207
BASN208
BSER209
BTRP214
BSER249
BPHE250
BHOH439
KHOH101

site_idAD6
Number of Residues23
Detailsbinding site for Ac-Asp-Glu-Val-Asp-CMK chain L
ChainResidue
CSER58
CARG64
CHIS121
CGLY122
CGLN161
CCYS163
CHOH404
CHOH465
DTYR204
DSER205
DTRP206
DARG207
DASN208
DSER209
DTRP214
DSER249
DPHE250
DHOH410
LHOH101
LHOH102
LHOH103
LHOH104
LHOH105

Functional Information from PROSITE/UniProt
site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HskrsSfvCvLLSHG
ChainResidueDetails
AHIS108-GLY122

site_idPS01122
Number of Residues12
DetailsCASPASE_CYS Caspase family cysteine active site. KPKLFIIQACRG
ChainResidueDetails
ALYS154-GLY165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120, ECO:0000269|PubMed:36423631
ChainResidueDetails
BARG207
DARG207
CHIS121
CCYS163

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1
CMET1

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P70677
ChainResidueDetails
ALYS11
CLYS11

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER26
CSER26

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine; in inhibited form => ECO:0000269|PubMed:10213689
ChainResidueDetails
ACYS163
CCYS163

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 815
ChainResidueDetails
ATHR62electrostatic stabiliser
ASER63electrostatic stabiliser
AHIS121electrostatic stabiliser, proton acceptor, proton donor
AGLY122electrostatic stabiliser
ACYS163electrostatic stabiliser

site_idMCSA2
Number of Residues
DetailsM-CSA 815
ChainResidueDetails
CTHR62electrostatic stabiliser
CSER63electrostatic stabiliser
CHIS121electrostatic stabiliser, proton acceptor, proton donor
CGLY122electrostatic stabiliser
CCYS163electrostatic stabiliser

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon