Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2Z86

Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0046872	molecular_function	metal ion binding
A	0047238	molecular_function	glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity
A	0050510	molecular_function	N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity
B	0003824	molecular_function	catalytic activity
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0046872	molecular_function	metal ion binding
B	0047238	molecular_function	glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity
B	0050510	molecular_function	N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity
C	0003824	molecular_function	catalytic activity
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0046872	molecular_function	metal ion binding
C	0047238	molecular_function	glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity
C	0050510	molecular_function	N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity
D	0003824	molecular_function	catalytic activity
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0046872	molecular_function	metal ion binding
D	0047238	molecular_function	glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity
D	0050510	molecular_function	N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 1

Chain	Residue
A	ARG161
A	ASP241
A	HIS386
A	HOH790

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MN A 2

Chain	Residue
A	ASP521

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN B 3

Chain	Residue
B	ASP241
B	HIS386
B	HOH820

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 4

Chain	Residue
B	HIS631
B	HOH821
B	HOH822
B	ASP521

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN C 5

Chain	Residue
C	ASP241
C	HIS386
C	HOH853

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN C 6

Chain	Residue
C	ASP521
C	HIS631
C	HOH795

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN D 7

Chain	Residue
D	ASP241
D	HIS386
D	HOH807

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN D 8

Chain	Residue
D	ASP521
D	HIS631

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE UDP B 1

Chain	Residue
B	PRO157
B	THR158
B	TYR159
B	ARG161
B	ASP188
B	TYR217
B	LEU219
B	ASP239
B	CYS240
B	ASP241
B	HIS386
B	HOH796
B	HOH798
B	HOH820

site_id	BC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE UGA B 683

Chain	Residue
B	ALA440
B	TYR441
B	ASP469
B	ASN496
B	GLY498
B	ILE499
B	GLN517
B	ASP519
B	SER520
B	ASP521
B	HIS581
B	ALA603
B	ASP605
B	ARG628
B	HIS631
B	HOH730
B	HOH822

site_id	BC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE UGA D 683

Chain	Residue
D	PRO157
D	THR158
D	TYR159
D	ARG161
D	ASP188
D	GLY216
D	TYR217
D	LEU219
D	ARG223
D	ASP239
D	ASP241
D	ARG268
D	GLY335
D	GLU361
D	ASP362
D	HIS386
D	HOH775
D	HOH780
D	HOH787
D	HOH807

site_id	BC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE UGA D 684

Chain	Residue
D	PRO439
D	TYR441
D	ASP469
D	ASN496
D	GLY498
D	ILE499
D	ALA502
D	GLN517
D	ASP519
D	SER520
D	ASP521
D	HIS581
D	ARG583
D	ASN602
D	ALA603
D	ASP605
D	ARG628
D	HOH776
D	HOH802

site_id	BC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE UDP C 1

Chain	Residue
C	LEU219
C	ASP239
C	CYS240
C	ASP241
C	HIS386
C	HOH819
C	HOH853
C	PRO157
C	THR158
C	TYR159
C	ARG161
C	ASP188
C	TYR217

site_id	BC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE UGA C 683

Chain	Residue
C	PRO439
C	TYR441
C	ASP469
C	ASN496
C	GLY498
C	ILE499
C	ALA502
C	GLN517
C	ASP519
C	SER520
C	ASP521
C	HIS581
C	ASN602
C	ALA603
C	ASP605
C	ARG628
C	HIS631
C	HOH787
C	HOH795
C	HOH811

site_id	BC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE UGA A 683

Chain	Residue
A	PRO157
A	THR158
A	TYR159
A	ARG161
A	ASP188
A	GLY216
A	TYR217
A	LEU219
A	ARG223
A	ASP239
A	CYS240
A	ARG268
A	GLU361
A	ASP362
A	HIS386
A	HOH735

site_id	BC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE UGA A 684

Chain	Residue
A	PRO439
A	TYR441
A	ASP469
A	ASN496
A	ILE499
A	GLN517
A	ASP519
A	SER520
A	HIS581
A	ARG583
A	ASN602
A	ALA603
A	ASP605

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18771653","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	264
Details	Region: {"description":"Glucuronosyltransferase; A2 domain","evidences":[{"source":"PubMed","id":"18771653","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1fr8

Chain	Residue	Details
A	GLU361
A	ASN363

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1fr8

Chain	Residue	Details
B	GLU361
B	ASN363

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1fr8

Chain	Residue	Details
C	GLU361
C	ASN363

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1fr8

Chain	Residue	Details
D	GLU361
D	ASN363

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