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1BBH

ATOMIC STRUCTURE OF A CYTOCHROME C' WITH AN UNUSUAL LIGAND-CONTROLLED DIMER DISSOCIATION AT 1.8 ANGSTROMS RESOLUTION

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 Residues13
DetailsBINDING SITE FOR RESIDUE HEC A 132
ChainResidue
AALA1
ACYS124
AHIS125
AARG129
AHOH769
AARG12
AGLN13
ATYR16
ATYR58
ATHR71
AARG72
APHE91
ACYS121

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEC B 132
ChainResidue
BARG12
BGLN13
BTYR16
BGLU17
BTYR58
BTHR71
BARG72
BPHE91
BCYS121
BCYS124
BHIS125
BARG129
BHOH764

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:8230224, ECO:0007744|PDB:1BBH
ChainResidueDetails
AARG12
AGLN13
AARG72
BARG12
BGLN13
BARG72

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: covalent => ECO:0000269|PubMed:8230224, ECO:0007744|PDB:1BBH
ChainResidueDetails
ACYS121
ACYS124
BCYS121
BCYS124

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:8230224, ECO:0007744|PDB:1BBH
ChainResidueDetails
AHIS125
BHIS125

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PDB entries from 2024-07-10

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