Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2G2P

Crystal Structure of E.coli transthyretin-related protein with bound Zn and Br

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006144	biological_process	purine nucleobase metabolic process
A	0016787	molecular_function	hydrolase activity
A	0032991	cellular_component	protein-containing complex
A	0033971	molecular_function	hydroxyisourate hydrolase activity
A	0042597	cellular_component	periplasmic space
A	0042802	molecular_function	identical protein binding
A	0051289	biological_process	protein homotetramerization
B	0006144	biological_process	purine nucleobase metabolic process
B	0016787	molecular_function	hydrolase activity
B	0032991	cellular_component	protein-containing complex
B	0033971	molecular_function	hydroxyisourate hydrolase activity
B	0042597	cellular_component	periplasmic space
B	0042802	molecular_function	identical protein binding
B	0051289	biological_process	protein homotetramerization
C	0006144	biological_process	purine nucleobase metabolic process
C	0016787	molecular_function	hydrolase activity
C	0032991	cellular_component	protein-containing complex
C	0033971	molecular_function	hydroxyisourate hydrolase activity
C	0042597	cellular_component	periplasmic space
C	0042802	molecular_function	identical protein binding
C	0051289	biological_process	protein homotetramerization
D	0006144	biological_process	purine nucleobase metabolic process
D	0016787	molecular_function	hydrolase activity
D	0032991	cellular_component	protein-containing complex
D	0033971	molecular_function	hydroxyisourate hydrolase activity
D	0042597	cellular_component	periplasmic space
D	0042802	molecular_function	identical protein binding
D	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1001

Chain	Residue
A	HIS9
A	HIS98
A	BR1021
A	HOH1109

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1002

Chain	Residue
B	HIS9
B	HIS98
B	BR1022
B	HOH1115

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1003

Chain	Residue
C	HIS98
C	BR1023
C	HOH1109
C	HIS9

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1004

Chain	Residue
D	HIS9
D	HIS98
D	BR1024
D	HOH1110

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1005

Chain	Residue
A	HIS96
A	HIS98
A	SER114
A	HOH1141

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1006

Chain	Residue
B	HIS96
B	HIS98
B	SER114
B	HOH1141

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C 1007

Chain	Residue
C	HIS96
C	HIS98
C	SER114

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN D 1008

Chain	Residue
D	HIS96
D	HIS98
D	SER114

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN A 1009

Chain	Residue
A	HIS96
A	SER114

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN B 1010

Chain	Residue
B	HIS96
B	SER114

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN D 1012

Chain	Residue
D	GLN3
D	HIS96
D	SER114

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 1013

Chain	Residue
A	ASP61
A	HIS89
A	HOH1136

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1014

Chain	Residue
B	ASP61
B	HIS89
B	HOH1144
D	ASP31

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C 1015

Chain	Residue
C	ASP61
C	HIS89
C	HOH1131

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1016

Chain	Residue
B	ASP31
D	ASP61
D	HIS89
D	HOH1107

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BR A 1021

Chain	Residue
A	VAL8
A	ARG47
A	HIS98
A	ZN1001

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BR B 1022

Chain	Residue
B	VAL8
B	ARG47
B	HIS98
B	ZN1002

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BR C 1023

Chain	Residue
C	VAL8
C	ARG47
C	HIS98
C	ZN1003

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BR D 1024

Chain	Residue
D	VAL8
D	ARG47
D	HIS98
D	ZN1004

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1100

Chain	Residue
A	TRP34
A	ARG63
A	HOH1126
B	TRP34
B	ARG63

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 1101

Chain	Residue
C	TRP34
C	ARG63
C	HOH1135
C	HOH1136
D	TRP34
D	ARG63

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1102

Chain	Residue
A	TYR111
A	GLY113
A	SER114
C	HIS9

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 1103

Chain	Residue
B	HIS9
B	SO41104
D	TYR111
D	GLY113
D	SER114

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 1104

Chain	Residue
B	HIS98
B	PRO100
B	TYR111
B	GLY113
B	SER114
D	SO41103

Functional Information from PROSITE/UniProt

site_id	PS00768
Number of Residues	16
Details	TRANSTHYRETIN_1 Transthyretin signature 1. HILNqqtGkPAadVtV

Chain	Residue	Details
A	HIS9-VAL24

site_id	PS00769
Number of Residues	13
Details	TRANSTHYRETIN_2 Transthyretin signature 2. YHVPllLSQYGYS

Chain	Residue	Details
A	TYR97-SER109

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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