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3R5K

A designed redox-controlled caspase-7

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 312
ChainResidue
ALYS76
AGLY89
ATHR90
AASP91
ALYS92

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 313
ChainResidue
AARG233
AHOH366
AARG87
ASER143
AHIS144
AGLN184

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 2
ChainResidue
ATYR211
ALYS212
BARG571
BGLU574
BLYS586

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 4
ChainResidue
BASP492
BTHR525
BVAL526
BTYR529
BGLN587
BILE588

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT B 5
ChainResidue
BLYS554
BSER602

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 7
ChainResidue
BARG387
BHIS444
BGLN484
BCYS486
BARG533

Functional Information from PROSITE/UniProt
site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HtnaaCfaCiLLSHG
ChainResidueDetails
AHIS131-GLY145

site_idPS01122
Number of Residues12
DetailsCASPASE_CYS Caspase family cysteine active site. KPKLFFIQACRG
ChainResidueDetails
ALYS177-GLY188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:15314233
ChainResidueDetails
AHIS144
BHIS444

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:11701129, ECO:0000269|PubMed:15314233, ECO:0000269|PubMed:16916640
ChainResidueDetails
ACYS186
BCYS486

site_idSWS_FT_FI3
Number of Residues6
DetailsSITE: Cleavage; by CAPN1 => ECO:0000269|PubMed:19617626
ChainResidueDetails
APHE36
AMET45
ASER47
BPHE336
BMET345
BSER347

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Involved in allosteric regulation => ECO:0000269|PubMed:15314233, ECO:0000269|PubMed:19581639
ChainResidueDetails
AARG187
ATYR223
BARG487
BTYR523

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
AALA2
BALA302

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207
ChainResidueDetails
ASER30
ASER239
BSER330
BSER539

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER37
BSER337

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PAK2 => ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207
ChainResidueDetails
ATHR173
BTHR473

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120
ChainResidueDetails
AARG233
BARG533

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PDB entries from 2024-10-30

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