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1FGA

REFINEMENT OF THE STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION AND ANALYSIS OF PRESUMED HEPARIN BINDING SITES BY SELENATE SUBSTITUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0008083molecular_functiongrowth factor activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SE4 A 147
ChainResidue
AASN27
ALYS119
AARG120
ALYS125
AHOH158
ABME302

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SE4 A 301
ChainResidue
ALYS135
AHOH183
AHOH219
ALYS52
AGLU59
AARG120

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 302
ChainResidue
ACYS69
AARG109
AARG120
ASE4147

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BME A 303
ChainResidue
AARG44
AGLN56
AGLU58
ASER64
AVAL88
ACYS92
APHE93

Functional Information from PROSITE/UniProt
site_idPS00247
Number of Residues24
DetailsHBGF_FGF HBGF/FGF family signature. GrLlAskcvtd.ECfFfErlesnnY
ChainResidueDetails
AGLY80-TYR103

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsMOD_RES: Symmetric dimethylarginine; alternate => ECO:0000250|UniProtKB:Q60487
ChainResidueDetails
AGLU99
AASN101
ATYR103

218853

PDB entries from 2024-04-24

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