Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5YBF

Crystal structure of the GluA2o LBD in complex with glutamate and HBT1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0015276	molecular_function	ligand-gated monoatomic ion channel activity
A	0016020	cellular_component	membrane
B	0015276	molecular_function	ligand-gated monoatomic ion channel activity
B	0016020	cellular_component	membrane
C	0015276	molecular_function	ligand-gated monoatomic ion channel activity
C	0016020	cellular_component	membrane
D	0015276	molecular_function	ligand-gated monoatomic ion channel activity
D	0016020	cellular_component	membrane
E	0015276	molecular_function	ligand-gated monoatomic ion channel activity
E	0016020	cellular_component	membrane
F	0015276	molecular_function	ligand-gated monoatomic ion channel activity
F	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue GLU A 901

Chain	Residue
A	TYR471
A	GLU726
A	TYR753
A	HOH1023
A	HOH1034
A	HOH1126
A	PRO499
A	LEU500
A	THR501
A	ARG506
A	LEU671
A	GLY674
A	SER675
A	THR676

site_id	AC2
Number of Residues	21
Details	binding site for residue 8SR A 902

Chain	Residue
A	ILE502
A	LYS514
A	PRO515
A	MET517
A	SER518
A	SER750
A	LYS751
A	GLY752
A	LEU772
A	ASN775
A	HOH1087
B	ILE502
B	LYS514
B	PRO515
B	MET517
B	SER518
B	SER750
B	LYS751
B	GLY752
B	LEU772
B	ASN775

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 903

Chain	Residue
A	GLU452
A	HIS456
C	GLU699
C	HOH2332

site_id	AC4
Number of Residues	14
Details	binding site for residue GLU B 901

Chain	Residue
B	TYR471
B	PRO499
B	LEU500
B	THR501
B	ARG506
B	LEU671
B	GLY674
B	SER675
B	THR676
B	GLU726
B	TYR753
B	HOH1016
B	HOH1020
B	HOH1025

site_id	AC5
Number of Residues	2
Details	binding site for residue ZN B 902

Chain	Residue
B	ASP475
B	HOH1018

site_id	AC6
Number of Residues	3
Details	binding site for residue ZN B 903

Chain	Residue
B	GLU452
B	LYS455
B	HIS456

site_id	AC7
Number of Residues	14
Details	binding site for residue GLU C 801

Chain	Residue
C	TYR471
C	PRO499
C	LEU500
C	THR501
C	ARG506
C	LEU671
C	GLY674
C	SER675
C	THR676
C	GLU726
C	TYR753
C	HOH2144
C	HOH2183
C	HOH2210

site_id	AC8
Number of Residues	3
Details	binding site for residue ZN C 802

Chain	Residue
C	HIS433
C	GLU440
C	HOH2339

site_id	AC9
Number of Residues	5
Details	binding site for residue ZN C 803

Chain	Residue
C	GLU452
C	HIS456
C	LEU774
C	GLN777
C	HOH2102

site_id	AD1
Number of Residues	5
Details	binding site for residue ACT C 804

Chain	Residue
C	ARG713
C	LYS720
C	TYR721
C	HOH2250
C	HOH2326

site_id	AD2
Number of Residues	24
Details	binding site for residue 8SR C 805

Chain	Residue
D	PRO515
D	MET517
D	SER518
D	SER750
D	LYS751
D	GLY752
D	LEU772
D	ASN775
D	HOH1012
D	HOH1055
C	ILE502
C	LYS514
C	PRO515
C	MET517
C	SER518
C	SER750
C	LYS751
C	GLY752
C	LEU772
C	ASN775
C	HOH2115
C	HOH2146
D	ILE502
D	LYS514

site_id	AD3
Number of Residues	14
Details	binding site for residue GLU D 901

Chain	Residue
D	TYR471
D	PRO499
D	LEU500
D	THR501
D	ARG506
D	LEU671
D	GLY674
D	SER675
D	THR676
D	GLU726
D	TYR753
D	HOH1041
D	HOH1049
D	HOH1140

site_id	AD4
Number of Residues	3
Details	binding site for residue ZN D 902

Chain	Residue
D	HIS433
D	GLU440
D	HOH1243

site_id	AD5
Number of Residues	4
Details	binding site for residue ZN D 903

Chain	Residue
D	GLU452
D	HIS456
D	LEU774
D	HOH1234

site_id	AD6
Number of Residues	5
Details	binding site for residue ACT D 904

Chain	Residue
D	ARG713
D	LYS720
D	TYR721
D	HOH1128
D	HOH1236

site_id	AD7
Number of Residues	4
Details	binding site for residue ZN D 905

Chain	Residue
D	GLU699
D	HOH1238
E	GLU452
E	HIS456

site_id	AD8
Number of Residues	14
Details	binding site for residue GLU E 901

Chain	Residue
E	TYR471
E	PRO499
E	LEU500
E	THR501
E	ARG506
E	LEU671
E	GLY674
E	SER675
E	THR676
E	GLU726
E	TYR753
E	HOH1028
E	HOH1035
E	HOH1153

site_id	AD9
Number of Residues	24
Details	binding site for residue 8SR E 902

Chain	Residue
E	ILE502
E	LYS514
E	PRO515
E	MET517
E	SER518
E	SER750
E	LYS751
E	GLY752
E	LEU772
E	ASN775
E	HOH1009
E	HOH1073
E	HOH1125
F	ILE502
F	LYS514
F	PRO515
F	MET517
F	SER518
F	SER750
F	LYS751
F	GLY752
F	LEU772
F	ASN775
F	HOH1039

site_id	AE1
Number of Residues	14
Details	binding site for residue GLU F 901

Chain	Residue
F	TYR471
F	PRO499
F	LEU500
F	THR501
F	ARG506
F	LEU671
F	GLY674
F	SER675
F	THR676
F	GLU726
F	TYR753
F	HOH1010
F	HOH1021
F	HOH1024

site_id	AE2
Number of Residues	2
Details	binding site for residue ZN F 902

Chain	Residue
F	ASP475
F	HOH1013

site_id	AE3
Number of Residues	3
Details	binding site for residue ZN F 903

Chain	Residue
F	GLU452
F	LYS455
F	HIS456

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:20614889, ECO:0007744\|PDB:2XHD

Chain	Residue	Details
A	PRO499
C	THR501
C	SER675
C	THR676
D	PRO499
D	THR501
D	SER675
D	THR676
E	PRO499
E	THR501
E	SER675
A	THR501
E	THR676
F	PRO499
F	THR501
F	SER675
F	THR676
A	SER675
A	THR676
B	PRO499
B	THR501
B	SER675
B	THR676
C	PRO499

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:20614889, ECO:0000269\|PubMed:21531559, ECO:0007744\|PDB:2XHD, ECO:0007744\|PDB:3R7X

Chain	Residue	Details
A	ARG506
B	ARG506
C	ARG506
D	ARG506
E	ARG506
F	ARG506

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:20614889, ECO:0000269\|PubMed:21531559, ECO:0007744\|PDB:2XHD

Chain	Residue	Details
A	GLU726
B	GLU726
C	GLU726
D	GLU726
E	GLU726
F	GLU726

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphoserine; by PKC => ECO:0000250\|UniProtKB:P19491

Chain	Residue	Details
A	SER683
B	SER683
C	SER683
D	SER683
E	SER683
F	SER683

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphoserine; by PKG => ECO:0000250\|UniProtKB:P19491

Chain	Residue	Details
A	SER717
B	SER717
C	SER717
D	SER717
E	SER717
F	SER717

site_id	SWS_FT_FI6
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN413
B	ASN413
C	ASN413
D	ASN413
E	ASN413
F	ASN413

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