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256B

IMPROVEMENT OF THE 2.5 ANGSTROMS RESOLUTION MODEL OF CYTOCHROME B562 BY REDETERMINING THE PRIMARY STRUCTURE AND USING MOLECULAR GRAPHICS

Replaces:  156B
Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0005506molecular_functioniron ion binding
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0022900biological_processelectron transport chain
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 107
ChainResidue
BLYS59
BARG62
BHOH523

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 108
ChainResidue
BLYS95
BARG98
BHOH624

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 107
ChainResidue
ALYS59
AARG62
AHOH506

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 108
ChainResidue
ALYS95
AARG98
AHOH622

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM A 109
ChainResidue
AGLU4
AMET7
AGLU8
APRO45
APHE61
APHE65
AARG98
ATYR101
AHIS102
ATYR105
AARG106
AHOH540
AHOH733

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEM B 109
ChainResidue
BGLU4
BMET7
BPRO46
BPHE61
BPHE65
BARG98
BTYR101
BHIS102
BTYR105
BARG106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
AMET7
AHIS102
BMET7
BHIS102

218500

PDB entries from 2024-04-17

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