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2G2P

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0006144biological_processpurine nucleobase metabolic process
A0016787molecular_functionhydrolase activity
A0032991cellular_componentprotein-containing complex
A0033971molecular_functionhydroxyisourate hydrolase activity
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
A0051289biological_processprotein homotetramerization
B0006144biological_processpurine nucleobase metabolic process
B0016787molecular_functionhydrolase activity
B0032991cellular_componentprotein-containing complex
B0033971molecular_functionhydroxyisourate hydrolase activity
B0042597cellular_componentperiplasmic space
B0042802molecular_functionidentical protein binding
B0051289biological_processprotein homotetramerization
C0006144biological_processpurine nucleobase metabolic process
C0016787molecular_functionhydrolase activity
C0032991cellular_componentprotein-containing complex
C0033971molecular_functionhydroxyisourate hydrolase activity
C0042597cellular_componentperiplasmic space
C0042802molecular_functionidentical protein binding
C0051289biological_processprotein homotetramerization
D0006144biological_processpurine nucleobase metabolic process
D0016787molecular_functionhydrolase activity
D0032991cellular_componentprotein-containing complex
D0033971molecular_functionhydroxyisourate hydrolase activity
D0042597cellular_componentperiplasmic space
D0042802molecular_functionidentical protein binding
D0051289biological_processprotein homotetramerization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AHIS9
AHIS98
ABR1021
AHOH1109

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1002
ChainResidue
BHIS9
BHIS98
BBR1022
BHOH1115

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1003
ChainResidue
CHIS98
CBR1023
CHOH1109
CHIS9

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1004
ChainResidue
DHIS9
DHIS98
DBR1024
DHOH1110

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1005
ChainResidue
AHIS96
AHIS98
ASER114
AHOH1141

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1006
ChainResidue
BHIS96
BHIS98
BSER114
BHOH1141

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 1007
ChainResidue
CHIS96
CHIS98
CSER114

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN D 1008
ChainResidue
DHIS96
DHIS98
DSER114

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 1009
ChainResidue
AHIS96
ASER114

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN B 1010
ChainResidue
BHIS96
BSER114

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN D 1012
ChainResidue
DGLN3
DHIS96
DSER114

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 1013
ChainResidue
AASP61
AHIS89
AHOH1136

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1014
ChainResidue
BASP61
BHIS89
BHOH1144
DASP31

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 1015
ChainResidue
CASP61
CHIS89
CHOH1131

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1016
ChainResidue
BASP31
DASP61
DHIS89
DHOH1107

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR A 1021
ChainResidue
AVAL8
AARG47
AHIS98
AZN1001

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR B 1022
ChainResidue
BVAL8
BARG47
BHIS98
BZN1002

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR C 1023
ChainResidue
CVAL8
CARG47
CHIS98
CZN1003

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR D 1024
ChainResidue
DVAL8
DARG47
DHIS98
DZN1004

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1100
ChainResidue
ATRP34
AARG63
AHOH1126
BTRP34
BARG63

site_idCC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 1101
ChainResidue
CTRP34
CARG63
CHOH1135
CHOH1136
DTRP34
DARG63

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1102
ChainResidue
ATYR111
AGLY113
ASER114
CHIS9

site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 1103
ChainResidue
BHIS9
BSO41104
DTYR111
DGLY113
DSER114

site_idCC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1104
ChainResidue
BHIS98
BPRO100
BTYR111
BGLY113
BSER114
DSO41103

Functional Information from PROSITE/UniProt
site_idPS00768
Number of Residues16
DetailsTRANSTHYRETIN_1 Transthyretin signature 1. HILNqqtGkPAadVtV
ChainResidueDetails
AHIS9-VAL24

site_idPS00769
Number of Residues13
DetailsTRANSTHYRETIN_2 Transthyretin signature 2. YHVPllLSQYGYS
ChainResidueDetails
ATYR97-SER109

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS9
DHIS9
DARG47
DTYR111
AARG47
ATYR111
BHIS9
BARG47
BTYR111
CHIS9
CARG47
CTYR111

222036

PDB entries from 2024-07-03

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