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2R50

The crystal structure of nonsymbiotic corn hemoglobin 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0016491molecular_functionoxidoreductase activity
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0016491molecular_functionoxidoreductase activity
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 166
ChainResidue
BARG110
BTYR111
BHOH204
BHOH205
CPRO163
CASP164
CHOH195

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 166
ChainResidue
CARG110
CTYR111
BASP164
BHOH304

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 167
ChainResidue
CLYS130
CTRP138
CLYS143
CHOH276
CHOH281

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 166
ChainResidue
AARG110
ATYR111
DLYS162
DPRO163
DASP164

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 167
ChainResidue
AASP164
DARG110
DTYR111
DHOH230

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM A 166
ChainResidue
AMET53
APHE54
ALYS69
AHIS73
AARG103
ALEU104
ATHR107
AHIS108
ATYR111
AHIS117
ATHR121
AILE157
AHOH212
AHOH326

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM B 167
ChainResidue
BMET53
BPHE54
BLYS69
BHIS73
BARG103
BLEU104
BHIS108
BTYR111
BHIS117
BTHR121
BHOH191
BHOH283

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM C 168
ChainResidue
CMET53
CPHE56
CHIS73
CARG103
CLEU104
CTHR107
CHIS108
CTYR111
CHIS117
CTHR121
CLEU153
CHOH224

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEM D 168
ChainResidue
DLYS69
DHIS73
DMET80
DARG103
DLEU104
DTHR107
DHIS108
DTYR111
DVAL113
DHIS117
DTHR121

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY B 168
ChainResidue
BPHE39
BPHE40
BHIS73
BALA74
BVAL77
BHOH176

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY D 169
ChainResidue
DPHE40
DHIS73
DALA74
DVAL77
DHOH173

Functional Information from PROSITE/UniProt
site_idPS00208
Number of Residues12
DetailsPLANT_GLOBIN Plant hemoglobins signature. NPkLktHAmsvF
ChainResidueDetails
AASN67-PHE78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68168
ChainResidueDetails
ASER55
BSER55
CSER55
DSER55

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O04986
ChainResidueDetails
ALYS69
BLYS69
CLYS69
DLYS69

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|Ref.2, ECO:0007744|PDB:2R50
ChainResidueDetails
AHIS73
BHIS73
CHIS73
DHIS73

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|Ref.2, ECO:0007744|PDB:2R50
ChainResidueDetails
AARG103
ATHR107
BARG103
BTHR107
CARG103
CTHR107
DARG103
DTHR107

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|Ref.2, ECO:0007744|PDB:2R50
ChainResidueDetails
AHIS108
BHIS108
CHIS108
DHIS108

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Homodimerization => ECO:0000269|Ref.2, ECO:0007744|PDB:2R50
ChainResidueDetails
ALYS143
BLYS143
CLYS143
DLYS143

224201

PDB entries from 2024-08-28

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