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6BMG

Structure of Recombinant Dwarf Sperm Whale Myoglobin (Oxy)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005737cellular_componentcytoplasm
A0015671biological_processoxygen transport
A0016491molecular_functionoxidoreductase activity
A0016528cellular_componentsarcoplasm
A0019430biological_processremoval of superoxide radicals
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0098809molecular_functionnitrite reductase activity
B0004601molecular_functionperoxidase activity
B0005344molecular_functionoxygen carrier activity
B0005737cellular_componentcytoplasm
B0015671biological_processoxygen transport
B0016491molecular_functionoxidoreductase activity
B0016528cellular_componentsarcoplasm
B0019430biological_processremoval of superoxide radicals
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0098809molecular_functionnitrite reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue HEM A 201
ChainResidue
ALYS42
AHIS93
AHIS97
AILE99
ATYR103
AOXY202
AHOH304
AHOH330
AHOH341
AHOH344
BLYS77
APHE43
AARG45
AHIS64
ATHR67
AVAL68
AALA71
ALEU89
ASER92

site_idAC2
Number of Residues4
Detailsbinding site for residue OXY A 202
ChainResidue
APHE43
AHIS64
AVAL68
AHEM201

site_idAC3
Number of Residues5
Detailsbinding site for residue CD A 203
ChainResidue
AHIS35
AACT213
AACT214
BHIS116
BHOH338

site_idAC4
Number of Residues4
Detailsbinding site for residue CD A 204
ChainResidue
AHIS36
AGLU38
AASP126
AACT210

site_idAC5
Number of Residues7
Detailsbinding site for residue CD A 205
ChainResidue
AHIS12
ALYS16
AASP122
BHIS12
BLYS16
BASP122
BHOH374

site_idAC6
Number of Residues5
Detailsbinding site for residue CD A 206
ChainResidue
AHIS119
AASP122
AACT212
AHOH412
AHOH428

site_idAC7
Number of Residues5
Detailsbinding site for residue CD A 207
ChainResidue
AHIS116
AACT209
AACT211
AHOH357
BHIS35

site_idAC8
Number of Residues4
Detailsbinding site for residue CD A 208
ChainResidue
AMET0
AHIS81
AHOH425
AHOH438

site_idAC9
Number of Residues6
Detailsbinding site for residue ACT A 209
ChainResidue
AHIS116
AGLN128
ACD207
AACT211
AHOH384
BHIS35

site_idAD1
Number of Residues9
Detailsbinding site for residue ACT A 210
ChainResidue
AHIS36
AGLU38
APHE106
AASP126
ACD204
AHOH307
AHOH348
AHOH390
AHOH413

site_idAD2
Number of Residues6
Detailsbinding site for residue ACT A 211
ChainResidue
AHIS116
ACD207
AACT209
AHOH308
AHOH383
BHIS35

site_idAD3
Number of Residues5
Detailsbinding site for residue ACT A 212
ChainResidue
ALYS16
AHIS119
AASP122
ACD206
AHOH328

site_idAD4
Number of Residues6
Detailsbinding site for residue ACT A 213
ChainResidue
AHIS35
ACD203
AACT214
AHOH334
BHIS116
BGLN128

site_idAD5
Number of Residues5
Detailsbinding site for residue ACT A 214
ChainResidue
AHIS35
ACD203
AACT213
AHOH305
BHIS116

site_idAD6
Number of Residues18
Detailsbinding site for residue HEM B 201
ChainResidue
BILE99
BTYR103
BLEU104
BOXY202
BHOH305
BHOH313
BHOH357
BHOH370
BHOH388
BLYS42
BPHE43
BARG45
BHIS64
BVAL68
BLEU89
BSER92
BHIS93
BHIS97

site_idAD7
Number of Residues4
Detailsbinding site for residue OXY B 202
ChainResidue
BPHE43
BHIS64
BVAL68
BHEM201

site_idAD8
Number of Residues4
Detailsbinding site for residue CD B 203
ChainResidue
BHIS36
BGLU38
BASP126
BACT205

site_idAD9
Number of Residues3
Detailsbinding site for residue CD B 204
ChainResidue
BMET0
BHIS81
BHOH383

site_idAE1
Number of Residues8
Detailsbinding site for residue ACT B 205
ChainResidue
BHIS36
BGLU38
BPHE106
BASP126
BCD203
BHOH314
BHOH352
BHOH397

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|Ref.2, ECO:0007744|PDB:6BMG
ChainResidueDetails
AHIS64
BHIS64

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|Ref.2, ECO:0007744|PDB:6BMG
ChainResidueDetails
AHIS93
BHIS93

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76
ChainResidueDetails
ASER3
BSER3

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04247
ChainResidueDetails
ATHR67
BTHR67

218853

PDB entries from 2024-04-24

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