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1A2I

SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH) FERROCYTOCHROME C3, NMR, 20 STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0009061biological_processanaerobic respiration
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEC A 108
ChainResidue
ALYS3
ALYS29
ACYS30
ACYS33
AHIS34
ATYR43
AARG44
ALYS45
ACYS46
AHEC109
AHEC110
AALA4
APRO5
ALEU9
AMET11
APHE20
AHIS22
AHIS25
AVAL28

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEC A 109
ChainResidue
ACYS33
AHIS35
ALYS45
ACYS46
ACYS51
AHIS52
ASER61
AALA62
AHIS67
AVAL68
AASN73
ATHR74
ALYS75
APHE76
AHEC108

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEC A 110
ChainResidue
APHE20
ATHR24
AHIS25
AASP32
ACYS33
ALYS77
ACYS79
ACYS82
AHIS83
AVAL86
ALEU97
ALYS104
AHEC108

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEC A 111
ChainResidue
AMET11
AALA13
ATHR14
AGLN16
AVAL18
ATYR65
ATYR66
AHIS70
AVAL80
AHIS83
ALEU97
ATHR98
AGLY99
ACYS100
ACYS105
AHIS106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS22
AHIS25
AHIS34
AHIS35
AHIS52
AHIS70
AHIS83
AHIS106

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: covalent
ChainResidueDetails
ACYS30
ACYS33
ACYS46
ACYS51
ACYS79
ACYS82
ACYS100
ACYS105

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PDB entries from 2024-07-24

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