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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6QAJ

Structure of the tripartite motif of KAP1/TRIM28

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0008270	molecular_function	zinc ion binding
A	0009253	biological_process	peptidoglycan catabolic process
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0030430	cellular_component	host cell cytoplasm
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis
B	0003796	molecular_function	lysozyme activity
B	0008270	molecular_function	zinc ion binding
B	0009253	biological_process	peptidoglycan catabolic process
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0016998	biological_process	cell wall macromolecule catabolic process
B	0030430	cellular_component	host cell cytoplasm
B	0031640	biological_process	killing of cells of another organism
B	0042742	biological_process	defense response to bacterium
B	0044659	biological_process	viral release from host cell by cytolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 500

Chain	Residue
A	CYS65
A	CYS68
A	CYS88
A	CYS91

site_id	AC2
Number of Residues	5
Details	binding site for residue ZN A 501

Chain	Residue
A	CYS83
A	HIS85
A	CYS117
A	VAL119
A	CYS120

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 502

Chain	Residue
A	CYS209
A	HIS212
A	CYS229
A	CYS232

site_id	AC4
Number of Residues	5
Details	binding site for residue ZN A 503

Chain	Residue
A	CYS221
A	SER223
A	CYS224
A	HIS237
A	HIS240

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN B 501

Chain	Residue
B	CYS221
B	CYS224
B	HIS237
B	HIS240

site_id	AC6
Number of Residues	5
Details	binding site for residue ZN B 502

Chain	Residue
B	CYS209
B	VAL211
B	HIS212
B	CYS229
B	CYS232

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN B 503

Chain	Residue
B	CYS65
B	CYS68
B	CYS88
B	CYS91

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN B 504

Chain	Residue
B	CYS83
B	HIS85
B	CYS117
B	CYS120

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	GLU-96
B	GLU-96

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:1892846, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	ASP-87
B	ASP-87

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	LEU-75
A	PHE-3
B	LEU-75
B	PHE-3

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000303\|PubMed:7831309

Chain	Residue	Details
A	SER10
A	ASN25
B	SER10
B	ASN25

site_id	SWS_FT_FI5
Number of Residues	112
Details	ZN_FING: RING-type => ECO:0000255\|PROSITE-ProRule:PRU00175

Chain	Residue	Details
A	CYS65-LYS121
B	CYS65-LYS121

site_id	SWS_FT_FI6
Number of Residues	94
Details	ZN_FING: B box-type 1; atypical => ECO:0000255\|PROSITE-ProRule:PRU00024

Chain	Residue	Details
A	ASP148-THR195
B	ASP148-THR195

site_id	SWS_FT_FI7
Number of Residues	82
Details	ZN_FING: B box-type 2 => ECO:0000255\|PROSITE-ProRule:PRU00024

Chain	Residue	Details
A	GLU204-LEU245
B	GLU204-LEU245

site_id	SWS_FT_FI8
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00024

Chain	Residue	Details
A	CYS153
B	CYS156
B	CYS177
B	HIS181
B	CYS209
B	HIS212
B	CYS232
B	HIS237
A	CYS156
A	CYS177
A	HIS181
A	CYS209
A	HIS212
A	CYS232
A	HIS237
B	CYS153

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER138
B	SER138

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q62318

Chain	Residue	Details
A	LYS266
B	LYS266

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS304
A	LYS377
B	LYS304
B	LYS377

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS340
B	LYS340

site_id	SWS_FT_FI13
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS127
A	LYS272
A	LYS407
B	LYS127
B	LYS272
B	LYS407

site_id	SWS_FT_FI14
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:25218447, ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS199
A	LYS254
A	LYS261
A	LYS319
B	LYS199
B	LYS254
B	LYS261
B	LYS319

site_id	SWS_FT_FI15
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS304
B	LYS304

site_id	SWS_FT_FI16
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:25218447

Chain	Residue	Details
A	LYS366
B	LYS366

site_id	SWS_FT_FI17
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:25218447, ECO:0007744\|PubMed:25755297, ECO:0007744\|PubMed:25772364, ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS377
B	LYS377

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU-96	proton shuttle (general acid/base)
A	ASP-87	covalent catalysis

site_id	MCSA2
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
B	GLU-96	proton shuttle (general acid/base)
B	ASP-87	covalent catalysis

224004

PDB entries from 2024-08-21

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