Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2GNV

Crystal structure of non-symbiotic plant hemoglobin from rice, B10 mutant F40L

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0010167biological_processresponse to nitrate
A0016491molecular_functionoxidoreductase activity
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0071731biological_processresponse to nitric oxide
A0080033biological_processresponse to nitrite
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0010167biological_processresponse to nitrate
B0016491molecular_functionoxidoreductase activity
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0071731biological_processresponse to nitric oxide
B0080033biological_processresponse to nitrite
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM A 166
ChainResidue
AALA50
AVAL121
ATYR150
AHOH393
APHE54
AHIS73
AARG103
ALEU104
ATHR107
AHIS108
ATYR111
AHIS117

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM B 166
ChainResidue
BALA50
BLYS69
BHIS73
BMET80
BARG103
BLEU104
BTHR107
BHIS108
BTYR111
BHIS117
BPHE118
BVAL121
BTYR150
BLEU153
BHOH361

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DIO B 301
ChainResidue
BLEU40
BILE43
BLEU70
BHIS73

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DIO A 302
ChainResidue
APHE39
ALEU40
AHIS73

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DIO B 303
ChainResidue
BTRP25
BSER32
BILE35
BALA36
BPHE78

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DIO A 304
ChainResidue
ATRP25
ASER32
AILE35
AALA36
AALA74
APHE78
AHOH319

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 Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68168
ChainResidueDetails
ASER55
BSER55

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10986467, ECO:0000269|PubMed:16893175, ECO:0007744|PDB:1D8U, ECO:0007744|PDB:2GNV
ChainResidueDetails
ALYS69
BLYS69

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:10986467, ECO:0000269|PubMed:16893175, ECO:0007744|PDB:1D8U, ECO:0007744|PDB:2GNV, ECO:0007744|PDB:2GNW
ChainResidueDetails
AHIS73
BHIS73

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10986467, ECO:0000269|PubMed:16893175, ECO:0007744|PDB:1D8U, ECO:0007744|PDB:2GNV, ECO:0007744|PDB:2GNW
ChainResidueDetails
AARG103
ATHR107
BARG103
BTHR107

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:10986467, ECO:0000269|PubMed:16893175, ECO:0007744|PDB:1D8U, ECO:0007744|PDB:2GNV, ECO:0007744|PDB:2GNW
ChainResidueDetails
AHIS108
BHIS108

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Homodimerization => ECO:0000269|PubMed:10986467, ECO:0007744|PDB:1D8U
ChainResidueDetails
ALYS143
BLYS143

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon