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3QQR

Crystal structure of Parasponia hemoglobin; Differential Heme Coordination is Linked to Quaternary Structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0009399biological_processnitrogen fixation
A0015671biological_processoxygen transport
A0016491molecular_functionoxidoreductase activity
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0005344molecular_functionoxygen carrier activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0009399biological_processnitrogen fixation
B0015671biological_processoxygen transport
B0016491molecular_functionoxidoreductase activity
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 163
ChainResidue
ALEU50
AHIS105
AVAL110
AHIS114
APHE115
ATHR118
ATYR146
ALEU149
AHOH178
AHOH189
APHE51
ATYR53
ALYS66
AHIS70
ATHR73
AARG100
AILE101
AILE104

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM B 163
ChainResidue
BLEU50
BPHE51
BSER52
BHIS70
BARG100
BILE104
BHIS105
BTHR108
BVAL110
BHIS114
BPHE115
BTHR118
BLEU149
BILE153
BHOH221

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DIO A 164
ChainResidue
ALYS127
ATRP134
ALYS139
BHOH188

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DIO A 165
ChainResidue
AARG119
ALYS139
AASN140
AHOH194

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DIO B 164
ChainResidue
BLYS127
BTRP134
BLYS139

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DIO A 166
ChainResidue
APHE115
AGLU116
AARG119
ATYR146
AASP147
AVAL150
ALYS154
AHOH227

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DIO A 167
ChainResidue
AGLU12
AGLU13
AARG86
AHOH232
BSER52
BTYR53

Functional Information from PROSITE/UniProt
site_idPS00208
Number of Residues12
DetailsPLANT_GLOBIN Plant hemoglobins signature. NPkLkpHAttvF
ChainResidueDetails
AASN64-PHE75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21491905, ECO:0007744|PDB:3QQR
ChainResidueDetails
ASER52
AARG100
BSER52
BARG100

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O04986
ChainResidueDetails
ALYS66
BLYS66

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:21491905, ECO:0007744|PDB:3QQR
ChainResidueDetails
AHIS70
BHIS70

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:21491905, ECO:0007744|PDB:3QQR
ChainResidueDetails
AHIS105
BHIS105

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Homodimerization => ECO:0000269|PubMed:21491905, ECO:0007744|PDB:3QQR
ChainResidueDetails
ALYS139
BLYS139

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:3402445
ChainResidueDetails
ASER2
BSER2

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PDB entries from 2024-07-31

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