Structure of PDB 7xyr Chain A

Receptor sequence

>7xyrA (length=546) Species: 818 (Bacteroides thetaiotaomicron) [Search protein sequence]

IPRPEYPRPQFERTTWVNLNGTWTYEFDLDDSGKKRNLPTAKELSKTITV
PFCPESKLSGVNHTDFIKKMWYQRSLPIPADWSNKKILLHFGAVDYLAEI
YIDGRLVGFHNGGSSPFVIDISRIAKPGNSHNLVVSVSDDAKSGRQACGK
QSPEKNSFACFYTRVTGIWQTVWMEALSPCGLKSANTYPDIDNNQLIITP
EFYQISNDQTLEVTIYDSQKKVAQVTSKCANGSNLILPIKNIKLWSPETP
HLYDISYCVKDAKGQIIDEVKSYVGMRKVHIANGKFYLNNEPYFQRLVMN
QGYYPDGIWTAPTDEALKNDILLSKEAGFNGARLHQKFFEERFHYWADKL
GFITWGESPNWGMNPDDEVASRNLLSEWIEILERDRNHPSIITWAPLTVP
LSGTFARLVFDLQKLTKAIDPSRPFNDLTGSGFHFLTDIWSISTYEPDAT
RFALSLKPDKNQAAYANQPFIIGEFGGIVWEEDALFERIEKLINAIQSSG
IISGFCYTQFSDIEQEKNGIYTYDRQPKFEMERIRSIFEKIPSRPI

3D structure

PDB

7xyr Cystal Structure of Beta-glucuronidase from Bacteroides thetaiotaomicron

Chain

Resolution

2.0 Å

3D
structure

[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Enzyme Commision number

3.2.1.31: beta-glucuronidase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)
BS01	MG	A	R23 E25 D334	R3 E5 D314
BS02	MG	A	Y26 R33 E195	Y6 R13 E175
BS03	MG	A	Y121 I122 D123 G124 N152 V154	Y101 I102 D103 G104 N132 V134
BS04	MG	A	F72 C73 G327 T330	F52 C53 G307 T310
BS05	MG	A	F72 Y92 I188	F52 Y72 I168
BS06	MG	A	A113 V114 H130 G132 S135	A93 V94 H110 G112 S115
BS07	MG	A	M319 C547 T549	M299 C506 T508
BS08	MG	A	R353 T453 G454 E498	R333 T429 G430 E474
BS09	MG	A	S134 W329 K357	S114 W309 K337
BS10	MG	A	P325 D326	P305 D306
BS11	MG	A	P568 K569 F570	P527 K528 F529
BS12	MG	A	H364 T374 S410	H344 T354 S390
BS13	MG	A	A415 P416 L417 N450 D451 L452	A395 P396 L397 N426 D427 L428
BS14	MG	A	Q315 W375 T413 I463	Q295 W355 T393 I439
BS15	MG	A	E388 S391 T428 L432	E368 S371 T404 L408
BS16	MG	A	Y116 A167 E397	Y96 A147 E377
BS17	MG	A	R165 Q166 A390	R145 Q146 A370
BS18	MG	A	A161 G164 R165 Q166 G382	A141 G144 R145 Q146 G362
BS19	MG	A	L452 T453 S455 F457	L428 T429 S431 F433
BS20	MG	A	D159 Q171 V185	D139 Q151 V165
BS21	MG	A	R23 E25 T191	R3 E5 T171
BS22	MG	A	F111 G112 A113 Q190	F91 G92 A93 Q170

Gene Ontology

	Molecular Function
GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds

	Biological Process
GO:0005975	carbohydrate metabolic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:7xyr, PDBe:7xyr, PDBj:7xyr
PDBsum	7xyr
PubMed
UniProt	Q8A2L3

[Back to BioLiP]