5KYF

Crystal structure of USP7 catalytic domain [L299A] mutant in complex with ubiquitin

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0004843	molecular_function	cysteine-type deubiquitinase activity
B	0016579	biological_process	protein deubiquitination

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue GOL B 601

Chain	Residue
B	VAL370
B	GLU495
B	HOH749
B	HOH881

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site_id	AC2
Number of Residues	9
Details	binding site for residue GOL B 602

Chain	Residue
B	HOH740
B	HOH763
B	HOH889
C	ARG72
B	TRP285
B	GLU298
B	HOH701
B	HOH704
B	HOH731

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Functional Information from PROSITE/UniProt

site_id	PS00299
Number of Residues	26
Details	UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD

Chain	Residue	Details
C	LYS27-ASP52

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site_id	PS00972
Number of Residues	16
Details	USP_1 Ubiquitin specific protease (USP) domain signature 1. GLknqGAtCYMNSlLQ

Chain	Residue	Details
B	GLY215-GLN230

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site_id	PS00973
Number of Residues	18
Details	USP_2 Ubiquitin specific protease (USP) domain signature 2. YiLhAVlvHsGdnhg..GHY

Chain	Residue	Details
B	TYR448-TYR465

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	SITE: Interacts with activating enzyme

Chain	Residue	Details
C	ARG54
C	ARG72

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Essential for function

Chain	Residue	Details
C	HIS68

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291

Chain	Residue	Details
C	SER65

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457

Chain	Residue	Details
C	THR66

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742

Chain	Residue	Details
C	GLY76

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site_id	SWS_FT_FI6
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603

Chain	Residue	Details
C	LYS6

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site_id	SWS_FT_FI7
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Chain	Residue	Details
C	GLY76

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site_id	SWS_FT_FI8
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144

Chain	Residue	Details
C	LYS11
C	LYS48

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site_id	SWS_FT_FI9
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860

Chain	Residue	Details
C	LYS27

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site_id	SWS_FT_FI10
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127

Chain	Residue	Details
C	LYS29

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site_id	SWS_FT_FI11
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577

Chain	Residue	Details
C	LYS33

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site_id	SWS_FT_FI12
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106

Chain	Residue	Details
C	LYS63

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 789

Chain	Residue	Details
B	PHE234	electrostatic stabiliser
B	ARG239	nucleofuge, nucleophile, proton acceptor, proton donor
B	PHE480	proton acceptor, proton donor
B	ASN497	electrostatic stabiliser

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