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

2QL7

Crystal Structure of Caspase-7 with inhibitor AC-IEPD-CHO

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 Residues10
DetailsBINDING SITE FOR RESIDUE CIT D 850
ChainResidue
AARG187
DVAL592
BPRO227
BCYS290
BVAL292
CARG487
DHOH36
DHOH135
DTYR523
DPRO527

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR CHAIN E OF INHIBITOR AC-IEPD_CHO
ChainResidue
AVAL86
AARG87
AHIS144
AGLY145
AGLN184
ACYS186
BSER231
BTRP232
BARG233
BPRO235
BTRP240
BGLN276
BHOH335

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR CHAIN F OF INHIBITOR AC-IEPD_CHO
ChainResidue
CARG387
CHIS444
CGLY445
CGLN484
CCYS486
DTYR530
DSER531
DTRP532
DARG533
DPRO535
DTRP540
DSER575
DGLN576

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR CHAIN G OF QGHGE
ChainResidue
AGLN59
BGLN260
BTYR300
BSER302
CGLN359
DGLN560
DTYR600
DSER602
GHOH217

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
DetailsSITE: Involved in allosteric regulation => ECO:0000269|PubMed:15314233, ECO:0000269|PubMed:19581639
ChainResidueDetails
BTYR223
DTYR523

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120
ChainResidueDetails
BARG233
DARG533

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207
ChainResidueDetails
ASER47
CPHE336
CMET345
CSER347
BSER239
DSER539

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Involved in allosteric regulation => ECO:0000269|PubMed:15314233, ECO:0000269|PubMed:19581639
ChainResidueDetails
AARG187
CARG487

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207
ChainResidueDetails
ASER30
CSER330

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER37
CSER337

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PAK2 => ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207
ChainResidueDetails
ATHR173
CTHR473

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon