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1N9H

structure of microgravity-grown oxidized myoglobin mutant YQR (ISS6A)

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OH A 500
ChainResidue
ATYR29
AGLN64
AVAL68
AHEM200

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 300
ChainResidue
AALA53
AHOH571
AHOH628
ASER3
AGLU4
ALYS34
ATHR51
AGLU52

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 200
ChainResidue
ALYS42
APHE43
AARG45
AGLN64
AARG67
AVAL68
ALEU89
ASER92
AHIS93
AHIS97
AILE99
ATYR103
AOH500
AHOH529
AHOH530
AHOH567
AHOH600
AHOH642
AHOH654

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:7463482, ECO:0007744|PDB:1MBO
ChainResidueDetails
AGLN64

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:845959, ECO:0007744|PDB:4MBN, ECO:0007744|PDB:5MBN
ChainResidueDetails
AHIS93

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76
ChainResidueDetails
ASER3

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04247
ChainResidueDetails
AARG67

227344

PDB entries from 2024-11-13

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