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1KI0

The X-ray Structure of Human Angiostatin

Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE BCN A 335
ChainResidue
AARG115
AHOH548
AHOH571
AHOH636
AHIS198
AGLY199
AILE201
AGLU221
ATRP225
APHE227
AARG234
ATRP235

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCN A 336
ChainResidue
AARG117
AASP137
AASP139
ATRP144
AARG153
ATYR154
ATHR287
AHOH711
AHOH725

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BCN A 337
ChainResidue
AARG290
ALYS311
ATRP315
AHIS317
AARG324
ATRP325
AHOH516
AHOH839

Functional Information from PROSITE/UniProt
site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. YCRNpdndpqgpWC
ChainResidueDetails
ATYR132-CYS145
ATYR214-CYS226
ATYR304-CYS316

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AARG117
AASP139
AARG153

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Interacts with fibrin
ChainResidueDetails
AARG115
AARG117

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:3356193, ECO:0000269|PubMed:9054441
ChainResidueDetails
ASER249

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:3356193
ChainResidueDetails
AGLU289

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 425
ChainResidueDetails

227344

PDB entries from 2024-11-13

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