Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3RZW

Crystal Structure of the Monobody ySMB-9 bound to human SUMO1

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0001741	cellular_component	XY body
C	0003723	molecular_function	RNA binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005643	cellular_component	nuclear pore
C	0005654	cellular_component	nucleoplasm
C	0005730	cellular_component	nucleolus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006281	biological_process	DNA repair
C	0006355	biological_process	regulation of DNA-templated transcription
C	0008076	cellular_component	voltage-gated potassium channel complex
C	0008134	molecular_function	transcription factor binding
C	0010621	biological_process	negative regulation of transcription by transcription factor localization
C	0015459	molecular_function	potassium channel regulator activity
C	0016604	cellular_component	nuclear body
C	0016605	cellular_component	PML body
C	0016607	cellular_component	nuclear speck
C	0016925	biological_process	protein sumoylation
C	0019899	molecular_function	enzyme binding
C	0030578	biological_process	PML body organization
C	0031334	biological_process	positive regulation of protein-containing complex assembly
C	0031386	molecular_function	protein tag activity
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0031647	biological_process	regulation of protein stability
C	0031965	cellular_component	nuclear membrane
C	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
C	0032880	biological_process	regulation of protein localization
C	0034605	biological_process	cellular response to heat
C	0042308	biological_process	negative regulation of protein import into nucleus
C	0043392	biological_process	negative regulation of DNA binding
C	0043433	biological_process	negative regulation of DNA-binding transcription factor activity
C	0044388	molecular_function	small protein activating enzyme binding
C	0044389	molecular_function	ubiquitin-like protein ligase binding
C	0045759	biological_process	negative regulation of action potential
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	0050821	biological_process	protein stabilization
C	0060021	biological_process	roof of mouth development
C	0071276	biological_process	cellular response to cadmium ion
C	0086004	biological_process	regulation of cardiac muscle cell contraction
C	0090204	biological_process	protein localization to nuclear pore
C	0097165	cellular_component	nuclear stress granule
C	1902260	biological_process	negative regulation of delayed rectifier potassium channel activity
C	1903169	biological_process	regulation of calcium ion transmembrane transport
C	1990381	molecular_function	ubiquitin-specific protease binding
D	0001741	cellular_component	XY body
D	0003723	molecular_function	RNA binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005643	cellular_component	nuclear pore
D	0005654	cellular_component	nucleoplasm
D	0005730	cellular_component	nucleolus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006281	biological_process	DNA repair
D	0006355	biological_process	regulation of DNA-templated transcription
D	0008076	cellular_component	voltage-gated potassium channel complex
D	0008134	molecular_function	transcription factor binding
D	0010621	biological_process	negative regulation of transcription by transcription factor localization
D	0015459	molecular_function	potassium channel regulator activity
D	0016604	cellular_component	nuclear body
D	0016605	cellular_component	PML body
D	0016607	cellular_component	nuclear speck
D	0016925	biological_process	protein sumoylation
D	0019899	molecular_function	enzyme binding
D	0030578	biological_process	PML body organization
D	0031334	biological_process	positive regulation of protein-containing complex assembly
D	0031386	molecular_function	protein tag activity
D	0031625	molecular_function	ubiquitin protein ligase binding
D	0031647	biological_process	regulation of protein stability
D	0031965	cellular_component	nuclear membrane
D	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
D	0032880	biological_process	regulation of protein localization
D	0034605	biological_process	cellular response to heat
D	0042308	biological_process	negative regulation of protein import into nucleus
D	0043392	biological_process	negative regulation of DNA binding
D	0043433	biological_process	negative regulation of DNA-binding transcription factor activity
D	0044388	molecular_function	small protein activating enzyme binding
D	0044389	molecular_function	ubiquitin-like protein ligase binding
D	0045759	biological_process	negative regulation of action potential
D	0045892	biological_process	negative regulation of DNA-templated transcription
D	0050821	biological_process	protein stabilization
D	0060021	biological_process	roof of mouth development
D	0071276	biological_process	cellular response to cadmium ion
D	0086004	biological_process	regulation of cardiac muscle cell contraction
D	0090204	biological_process	protein localization to nuclear pore
D	0097165	cellular_component	nuclear stress granule
D	1902260	biological_process	negative regulation of delayed rectifier potassium channel activity
D	1903169	biological_process	regulation of calcium ion transmembrane transport
D	1990381	molecular_function	ubiquitin-specific protease binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL B 91

Chain	Residue
B	SER17
B	LEU18

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 92

Chain	Residue
B	TYR36
B	THR58
B	SER60
D	GLN92
D	GLN94

Functional Information from PROSITE/UniProt

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGNSP

Chain	Residue	Details
A	GLY37-PRO44

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	SITE: Interaction with PIAS2

Chain	Residue	Details
C	PHE36
D	PHE36

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:18707152, ECO:0007744\|PubMed:17081983, ECO:0007744\|PubMed:18691976, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	SER2
D	SER2

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:20068231

Chain	Residue	Details
C	SER9
D	SER9

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	SER32
D	SER32

site_id	SWS_FT_FI5
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
C	LYS7
D	LYS7

site_id	SWS_FT_FI6
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000269\|PubMed:27068747

Chain	Residue	Details
C	GLY97
D	GLY97

site_id	SWS_FT_FI7
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:25218447, ECO:0007744\|PubMed:28112733

Chain	Residue	Details
C	LYS16
D	LYS16

site_id	SWS_FT_FI8
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:25218447, ECO:0007744\|PubMed:25772364, ECO:0007744\|PubMed:28112733

Chain	Residue	Details
C	LYS17
D	LYS17

site_id	SWS_FT_FI9
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
C	LYS23
C	LYS39
C	LYS45
C	LYS46
D	LYS23
D	LYS39
D	LYS45
D	LYS46

site_id	SWS_FT_FI10
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)

Chain	Residue	Details
C	LYS25
D	LYS25

site_id	SWS_FT_FI11
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:25755297, ECO:0007744\|PubMed:28112733

Chain	Residue	Details
C	LYS37
D	LYS37

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)