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3OD5

Crystal structure of active caspase-6 bound with Ac-VEID-CHO

Functional Information from GO Data
ChainGOidnamespacecontents
A0002218biological_processactivation of innate immune response
A0004175molecular_functionendopeptidase activity
A0004197molecular_functioncysteine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006915biological_processapoptotic process
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0016540biological_processprotein autoprocessing
A0016787molecular_functionhydrolase activity
A0030855biological_processepithelial cell differentiation
A0042802molecular_functionidentical protein binding
A0043065biological_processpositive regulation of apoptotic process
A0043067biological_processregulation of programmed cell death
A0043525biological_processpositive regulation of neuron apoptotic process
A0051716biological_processcellular response to stimulus
A0060545biological_processpositive regulation of necroptotic process
A0070269biological_processpyroptosis
A0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
A0072734biological_processcellular response to staurosporine
A0097153molecular_functioncysteine-type endopeptidase activity involved in apoptotic process
A0097194biological_processexecution phase of apoptosis
A0097200molecular_functioncysteine-type endopeptidase activity involved in execution phase of apoptosis
A0097284biological_processhepatocyte apoptotic process
B0002218biological_processactivation of innate immune response
B0004175molecular_functionendopeptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0006915biological_processapoptotic process
B0008233molecular_functionpeptidase activity
B0008234molecular_functioncysteine-type peptidase activity
B0016540biological_processprotein autoprocessing
B0016787molecular_functionhydrolase activity
B0030855biological_processepithelial cell differentiation
B0042802molecular_functionidentical protein binding
B0043065biological_processpositive regulation of apoptotic process
B0043067biological_processregulation of programmed cell death
B0043525biological_processpositive regulation of neuron apoptotic process
B0051716biological_processcellular response to stimulus
B0060545biological_processpositive regulation of necroptotic process
B0070269biological_processpyroptosis
B0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
B0072734biological_processcellular response to staurosporine
B0097153molecular_functioncysteine-type endopeptidase activity involved in apoptotic process
B0097194biological_processexecution phase of apoptosis
B0097200molecular_functioncysteine-type endopeptidase activity involved in execution phase of apoptosis
B0097284biological_processhepatocyte apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CAC A 1
ChainResidue
ACYS264
CVAL301

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CAC A 3
ChainResidue
AARG164
ATYR210
AGLU214
ACYS277
AALA279
BALA279

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CAC A 7
ChainResidue
AALA69
AASP72
BCAC6
BASP72
ACYS68

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CAC A 8
ChainResidue
ATHR75
ACYS87
AHOH498
AHOH665

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CAC B 2
ChainResidue
BCYS264
DVAL301

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CAC B 4
ChainResidue
AGLU53
AARG54
AASP90
BASN51
BGLU53
BCYS68
BASN89

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CAC B 5
ChainResidue
AALA279
BARG164
BTYR210
BGLU214
BCYS277
BALA279

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CAC B 6
ChainResidue
ACAC7
BTHR75
BVAL85
BCYS87
BHOH750

site_idAC9
Number of Residues23
DetailsBINDING SITE FOR CHAIN C OF PEPTIDE ALDEHYDE INHIBITOR AC-VEID-CHO
ChainResidue
ACAC1
AARG64
AHIS121
AGLY122
AGLN161
ACYS163
ATYR217
ASER218
AHIS219
AARG220
AGLU221
ATHR222
AHOH326
AHOH764
CHOH39
CHOH100
CHOH255
CHOH353
CHOH383
CHOH438
CHOH646
CHOH696
CHOH791

site_idBC1
Number of Residues18
DetailsBINDING SITE FOR CHAIN D OF PEPTIDE ALDEHYDE INHIBITOR AC-VEID-CHO
ChainResidue
BCAC2
BARG64
BARG65
BHIS121
BGLN161
BCYS163
BTYR217
BSER218
BHIS219
BARG220
BGLU221
BTHR222
BHOH342
BHOH345
BHOH556
DHOH254
DHOH574
DHOH714

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:30420425
ChainResidueDetails
AHIS121
BHIS121

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:16123779, ECO:0000269|PubMed:19133298, ECO:0000269|PubMed:19694615, ECO:0000269|PubMed:20890311, ECO:0000269|PubMed:28864531, ECO:0000269|PubMed:30420425
ChainResidueDetails
ACYS163
BCYS163

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08738
ChainResidueDetails
ASER79
BSER79

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by NUAK1 and AMPK => ECO:0000269|PubMed:15273717, ECO:0000269|PubMed:22483120, ECO:0000269|PubMed:32029622
ChainResidueDetails
ASER257
BSER257

site_idSWS_FT_FI5
Number of Residues4
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27911442
ChainResidueDetails
ACYS264
ACYS277
BCYS264
BCYS277

218853

PDB entries from 2024-04-24

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