2QL9

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004197	molecular_function	cysteine-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	0008234	molecular_function	cysteine-type peptidase activity
B	0004197	molecular_function	cysteine-type endopeptidase activity
B	0006508	biological_process	proteolysis
B	0008234	molecular_function	cysteine-type peptidase activity
C	0004197	molecular_function	cysteine-type endopeptidase activity
C	0006508	biological_process	proteolysis
C	0008234	molecular_function	cysteine-type peptidase activity
D	0004197	molecular_function	cysteine-type endopeptidase activity
D	0006508	biological_process	proteolysis
D	0008234	molecular_function	cysteine-type peptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT D 850

Chain	Residue
A	ARG187
B	PRO227
B	CYS290
C	ARG487
D	TYR523
D	PRO527
D	CYS590
D	VAL592

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR CHAIN E OF INHIBITOR AC-DQMD-CHO

Chain	Residue
A	HIS144
A	GLY145
A	GLN184
A	CYS186
B	HOH51
B	TYR230
B	SER231
B	TRP232
B	ARG233
B	SER234
B	PRO235
B	SER275
B	GLN276
B	PHE282
E	HOH104
A	ARG87

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR CHAIN F OF INHIBITOR AC-DQMD-CHO

Chain	Residue
C	HOH271
C	ARG387
C	HIS444
C	GLY445
C	GLN484
C	CYS486
D	SER531
D	TRP532
D	ARG533
D	SER534
D	PRO535
D	SER575
D	GLN576
D	PHE582
F	HOH56
F	HOH89
F	HOH153

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR CHAIN G OF PEPTIDE QGHGE

Chain	Residue
A	GLN59
B	GLN260
B	TYR300
B	SER302
B	GLN303
B	HOH353
C	GLN359
D	GLN560
D	TYR600
D	SER602
G	HOH289

---

Functional Information from PROSITE/UniProt

site_id	PS01121
Number of Residues	15
Details	CASPASE_HIS Caspase family histidine active site. HtnaaCfaCiLLSHG

Chain	Residue	Details
A	HIS131-GLY145

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site_id	PS01122
Number of Residues	12
Details	CASPASE_CYS Caspase family cysteine active site. KPKLFFIQACRG

Chain	Residue	Details
A	LYS177-GLY188

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	SITE: Involved in allosteric regulation => ECO:0000269|PubMed:15314233, ECO:0000269|PubMed:19581639

Chain	Residue	Details
B	TYR223
D	TYR523

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120

Chain	Residue	Details
B	ARG233
D	ARG533

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207

Chain	Residue	Details
B	SER239
D	SER539
A	SER47
C	PHE336
C	MET345
C	SER347

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Involved in allosteric regulation => ECO:0000269|PubMed:15314233, ECO:0000269|PubMed:19581639

Chain	Residue	Details
A	ARG187
C	ARG487

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207

Chain	Residue	Details
A	SER30
C	SER330

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER37
C	SER337

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PAK2 => ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207

Chain	Residue	Details
A	THR173
C	THR473

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1qx3

Chain	Residue	Details
A	CYS186
A	GLY145
A	HIS144

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1qx3

Chain	Residue	Details
C	GLY445
C	HIS444
C	CYS486

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